Product Name
alpha-Spectrin (SPTA1), Polyclonal Antibody
Full Product Name
alpha-Spectrin Antibody
Product Synonym Names
alpha-Spectrin
Product Gene Name
anti-SPTA1 antibody
[Similar Products]
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Chromosome Location
Chromosome: 1; NC_000001.10 (158580496..158656506, complement). Location: 1q21
3D Structure
ModBase 3D Structure for P02549
Purity/Purification
Affinity purified
Concentration
100ug/100ul (lot specific)
Immunogen
The spectrin family of proteins were originally discovered as major components of the submembraneous cytoskeleton of osmotically lyzed red blood cells. The lyzed blood cells could be seen as clear red blood cell shaped objects in the light microscope and were referred to as red blood cell "ghosts". The major proteins of red blood cell ghosts proved to be actin, ankyrin, band 4.1 and several other proteins, including a closely spaced pair of bands running at about 240 and 260kDa on SDS-PAGE gels. This pair of bands was named "spectrin" since they were discovered in these red blood cell ghosts (1). Later work showed that similar high molecular bands were seen in membrane preparations from other eukaryotic cell types. Work by Levine and Willard described a pair of about ~240-260 kDa molecular weight bands which were transported at the slowest rate along mammalian axons. They named these proteins "fodrin" as antibody studies showed that they were localized in the sheath under the axonal membrane, but not in the core of the axon (2; fodros is Greek for sheath). Subsequently fodrin was found to be a member of the spectrin family of proteins, and the spectrin nomenclature is now normally used (3). Spectrins form tetramers of two alpha and two beta subunits, with the alpha corresponding to the lower molecular weight ~240kDa band and the beta corresponding to the ~260kDa or in some case much larger band. Most spectrin tetramers are ~0.2m long, and each alpha and beta subunit has a cell type specific expression pattern. The basic structure of each spectrin subunit is the spectrin repeat, which is a sequence of about 110 amino acids which defines a compact domain contain three closely packed alpha-helices. Each spectrin subunit contains multiple copies of this repeat, with 20 in each of the alpha subunits. The beta I-IV subunits each contain 17 spectrin repeats, while the beta V subunit, also known as beta-heavy spectrin, contains 30 of these repeats. The various subunits also contain several other kinds of functional domain, allowing the spectrin tetramer to interact with a variety of protein, ionic and lipid targets. The alpha-subunits each contain one calmodulin like calcium binding region and one Src-homology 3 (SH3) domain, an abundant domain involved in specific protein-protein interactions. The beta subunits all have a N-terminal actin binding domain and may also have one SH3 domain and one pleckstrin homology domain, a multifunctional type of binding domain which in beta I spectrin at least binds the membrane lipid PIP2 (5). Spectrins are believed to have a function in giving mechanical strength to the plasma membrane since the tetramers associate with each other to form a dense submembraneous geodesic meshwork (3). They also bind a variety of other membrane proteins and membrane lipids, and the proteins they bind to are therefore themselves localized in the membrane. Diseases may be associated with defects in one or other of the spectrin subunits (6). For example, some forms of hereditary spherocytosis, the presence of spherical red blood cells which are prone to lysis, can be traced to mutations in some of the spectrin subunits (7). As another example, various mutations altering either the actin binding domain or repeat three of bIII spectrin are causative of one form spinocerebellar ataxia, SCA5 (8). The alpha-II subunit is widely expressed in tissues but, in the nervous system, is found predominantly in neurons. Our antibody can therefore be used to identify neurons and fragments derived from neuronal membranes in cells in tissue culture and in sectioned material. This antibody was raised against a recombinant construct containing the seventh, eight and ninth of the so-called spectrin repeats. The HGNC name for this protein is SPTAN1.
Storage Buffer
PBS, pH 7.4 with 0.02% sodium azide.
Preparation and Storage
This product is stable for several weeks at 4 degree C as an undiluted liquid. Dilute only prior to immediate use. For extended storage, aliquot contents and freeze at -20 degree C or below. Avoid cycles of freezing and thawing. Expiration date is one (1) year from date of receipt.
Other Notes
Small volumes of anti-SPTA1 antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
Related Product Information for
anti-SPTA1 antibody
alpha-Spectrin is a The spectrins, including nonerythrocytic alpha-spectrin-1 (SPTAN1), are a family of widely-distributed filamentous cytoskeletal proteins with have a highly conserved 106-amino acid repeat structure. Spectrins are heterodimers of a constant alpha-chain and variable, tissue-specific beta-chains. Functions of these proteins include regulation of receptor binding and actin crosslinking (Leto et al., 1988).
Applications Tested/Suitable for anti-SPTA1 antibody
Immunofluorescence (IF), Western Blot (WB)
Application Notes for anti-SPTA1 antibody
On western blots look for a major band at 240kDa, depending on the species.
1:250-500 for immunofluorescence staining and 1:2500-5000 for western blotting.
Western Blot (WB) of anti-SPTA1 antibody
NCBI/Uniprot data below describe general gene information for SPTA1. It may not necessarily be applicable to this product.
NCBI Accession #
AAA60994.1
[Other Products]
UniProt Primary Accession #
P02549
[Other Products]
UniProt Secondary Accession #
Q15514; Q5VYL1; Q5VYL2; Q6LDY5[Other Products]
UniProt Related Accession #
P02549[Other Products]
Molecular Weight
280,014 Da[Similar Products]
NCBI Official Full Name
alpha-spectrin
NCBI Official Synonym Full Names
spectrin, alpha, erythrocytic 1 (elliptocytosis 2)
NCBI Official Symbol
SPTA1??[Similar Products]
NCBI Official Synonym Symbols
EL2; HPP; HS3; SPH3; SPTA
??[Similar Products]
NCBI Protein Information
spectrin alpha chain, erythrocytic 1; alpha-I spectrin; erythroid alpha-spectrin; spectrin alpha chain, erythrocyte
UniProt Protein Name
Spectrin alpha chain, erythrocytic 1
UniProt Synonym Protein Names
Erythroid alpha-spectrin
UniProt Gene Name
SPTA1??[Similar Products]
UniProt Synonym Gene Names
SPTA??[Similar Products]
UniProt Entry Name
SPTA1_HUMAN
NCBI Summary for SPTA1
Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is a tetramer made up of alpha-beta dimers linked in a head-to-head arrangement. This gene is one member of a family of alpha-spectrin genes. The encoded protein is primarily composed of 22 spectrin repeats which are involved in dimer formation. It forms weaker tetramer interactions than non-erythrocytic alpha spectrin, which may increase the plasma membrane elasticity and deformability of red blood cells. Mutations in this gene result in a variety of hereditary red blood cell disorders, including elliptocytosis type 2, pyropoikilocytosis, and spherocytic hemolytic anemia. [provided by RefSeq, Jul 2008]
UniProt Comments for SPTA1
Function: Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane.
Subunit structure: Composed of non-homologous chains, alpha and beta, which aggregate side-to-side in an antiparallel fashion to form dimers, tetramers, and higher polymers. Interacts with FASLG. Ref.12 Ref.14
Subcellular location: Cytoplasm ? cytoskeleton. Cytoplasm ? cell cortex.
Involvement in disease: Elliptocytosis 2 (EL2) [MIM:130600]: A Rhesus-unlinked form of hereditary elliptocytosis, a genetically heterogeneous, autosomal dominant hematologic disorder. It is characterized by variable hemolytic anemia and elliptical or oval red cell shape.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.22 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28Hereditary pyropoikilocytosis (HPP) [MIM:266140]: Autosomal recessive hematologic disorder characterized by hemolytic anemia, microspherocytosis, poikilocytosis, and an unusual thermal sensitivity of red cells.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18Spherocytosis 3 (SPH3) [MIM:270970]: Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. SPH3 is characterized by severe hemolytic anemia. Inheritance is autosomal recessive.Note: The disease is caused by mutations affecting the gene represented in this entry.
Miscellaneous: This complex is anchored to the cytoplasmic face of the plasma membrane via another protein, ankyrin, which binds to beta-spectrin and mediates the binding of the whole complex to a transmembrane protein band 3. The interaction of erythrocyte spectrin with other proteins through specific binding domains lead to the formation of an extensive subplasmalemmal meshwork which is thought to be responsible for the maintenance of the biconcave shape of human erythrocytes, for the regulation of plasma membrane components and for the maintenance of the lipid asymmetry of the plasma membrane.
Sequence similarities: Belongs to the spectrin family.Contains 3 EF-hand domains.Contains 1 SH3 domain.Contains 21 spectrin repeats.
Product References and Citations for anti-SPTA1 antibody
1. Marchesi VT & Steers E Jr. Selective solubilization of a protein component of the red cell membrane. Science 159:203-4 (1968).2. Levine J & Willard M. Fodrin: axonally transported polypeptides associated with the internal periphery of many cells. J Cell Biol. 90:631-42 (1981).3. Bennett V & Baines AJ. Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues. Physiol Rev. 81:1353-92 (2001).4. Djinovic-Carugo K, Gautel M, Yl nne J & Young P. The spectrin repeat: a structural platform for cytoskeletal protein assemblies. FEBS Lett. 513:119-23 (2002).5. Wang, DS and Shaw G. The association of the C-terminal region of beta I sigma II spectrin to brain membranes is mediated by a PH domain, does not require membrane proteins, and coincides with a inositol-1,4,5 triphosphate . BBRC 217:608-15 (1995).6. Bennett V & Healy J. Organizing the fluid membrane bilayer: diseases linked to spectrin and ankyrin. Trends Mol Med 14:28-36 (2008).7. Eber S & Lux SE. Hereditary spherocytosis--defects in proteins that connect the membrane skeleton to the lipid bilayer. Semin Hematol 41:118-41 (2004).8. Ikeda Y. et al. Spectrin mutations cause spinocerebellar ataxia type 5. Nature Genetics 38:184-90 (2006).
Research Articles on SPTA1
1. The unusually slow, two-state kinetics of spectrin assembly in solution, was investigated.
Precautions
All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.
Disclaimer
While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.
It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.
