HAP; BAG family molecular chaperone regulator 1

For Research Use Only. Not for use in diagnostic procedures.

E Coli

> 95%

Freeze-dried powder

Avoid repeated freeze/thaw cycles. Store at 2-8 degree C for one month. Aliquot and store at -80 degree C for 12 months.
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37 degree C for 48h, and no obvious degradation and precipitation were observed. The loss rate is less than 5% within the expiration date under appropriate storage condition.

Manufactured in an ISO 9001:2008 and ISO 13485:2003 Certified Laboratory.

Manufactured in a lab with traceable raw materials. Bulk orders can typically be prepared to the customera??s specifications, please inquire.

Small volumes of BAG1 recombinant protein 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.

Recombinant Protein

Positive Control, Immunogen, SDS-PAGE, Western Blot (WB)

24.3kDa

BCL2-associated athanogene 1

BAG family molecular chaperone regulator 1

BAG family molecular chaperone regulator 1

BAG-1??[Similar Products]

The oncogene Bcl2 encodes a membrane protein that blocks a step in a pathway leading to apoptosis or programmed cell death. The protein encoded by this gene binds to Bcl2 protein and is referred to as Bcl2-associated athanogene. It enhances the anti-apoptotic effects of Bcl2 and represents a link between growth factor receptors and anti-apoptotic mechanisms. At least two protein isoforms are encoded by this mRNA through the use of a non-AUG (CUG) start site and an alternative, downstream, AUG translation initiation site. [provided by RefSeq, Jul 2008]

BAG1: Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity. Markedly increases the anti-cell death function of BCL2 induced by various stimuli. Homodimer. Forms a heteromeric complex with HSP70/HSC70. Binds to the ATPase domain of HSP/HSC70 chaperones. Isoform 1, isoform 3 and isoform 4 but not isoform 2 interact with HSPA8/HSC70. Interacts with NR3C1. Interacts with the N-terminal region of STK19. Interacts with PPP1R15A. Interacts with BCL2 in an ATP-dependent manner. Isoform 2 does not interact with BCL2. Up-regulated during differentiation of bladder epithelial cells and down-regulated during differentiation of prostate epithelium. Isoform 4 is the most abundantly expressed isoform. It is ubiquitously expressed throughout most tissues, except the liver, colon, breast and uterine myometrium. Isoform 1 is expressed in the ovary and testis. Isoform 4 is expressed in several types of tumor cell lines, and at consistently high levels in leukemia and lymphoma cell lines. Isoform 1 is expressed in the prostate, breast and leukemia cell lines. Isoform 3 is the least abundant isoform in tumor cell lines. 4 isoforms of the human protein are produced by alternative splicing.

Protein type: Motility/polarity/chemotaxis; Nuclear receptor co-regulator

Chromosomal Location of Human Ortholog: 4|4 A5

Cellular Component: cytoplasm; cytosol; mitochondrion; nucleus; perinuclear region of cytoplasm

Molecular Function: phosphoprotein binding; protein binding

Biological Process: negative regulation of apoptosis; negative regulation of protein amino acid phosphorylation; neuron differentiation; positive regulation of neuron apoptosis; positive regulation of transcription from RNA polymerase II promoter

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