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Heat shock 70 kDa protein 1B (HSPA1B) Antibody [HSPA1B/7628]

Additional information

Catalog Number: 3304-MSM8
Host:

Reactivity:

Gene:

In Stock

Trial Size Available

Carrier-Free Available

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In Stock
Catalog Number Formulation Size Price
3304-MSM8-P0
Purified Ab with BSA and Azide at 200ug/ml
20ug
$259.00
3304-MSM8-P1
Purified Ab with BSA and Azide at 200ug/ml
100ug
$559.00
3304-MSM8-P1ABX
Purified Ab WITHOUT BSA or Azide at 1.0mg/ml
100ug
$559.00
Flat Rate Domestic: $95 | Orders outside the US - Contact Us for Order Information | Ships next business day
Heat shock 70 kDa protein 1B (HSPA1B) Antibody

Formalin-fixed, paraffin-embedded human breast carcinoma stained with HSPA1B Mouse Monoclonal Antibody (HSPA1B/7628). HIER: Tris/EDTA, pH9.0, 45min. 2°C: HRP-polymer, 30min. DAB, 5min.

Heat shock 70 kDa protein 1B (HSPA1B) Antibody - Image 2

Formalin-fixed, paraffin-embedded human salivary gland stained with HSPA1B Mouse Monoclonal Antibody (HSPA1B/7628). HIER: Tris/EDTA, pH9.0, 45min. 2°C: HRP-polymer, 30min. DAB, 5min.

  • IHC
  • Documents
  • Applications & Dilutions
  • Product Properties
  • other information

Documents

Document Name
Datasheet Download Here
Material Safety Data Sheet Download Here

Applications & Dilutions

Applications Tested Dilutions Protocol Note
Immunohistochemistry (IHC) 1-2ug/ml IHC Protocol 30 min at RT. Staining of formalin-fixed tissues requires heating tissue sections in 10mM Tris with 1mM EDTA, pH 9.0, for 45 min at 95°C followed by cooling at RT for 20 minutes

Product Properties

Antibody Type
Mouse Monoclonals
Host
Mouse
Applications
Immunohistochemistry
Species Reactivity
Human
Clone
HSPA1B/7628
Isotype
IgG1
Light Chain
Lambda
Cellular Localization
Cytoplasm. Nucleus.
Gene Name
HSPA1B
Positive Control
Human testis or breast cancer.
Immunogen
Recombinant fragment (around aa400-600) of human HSPA1B protein (exact sequence is proprietary)
Storage & Stability
Antibody with azide - store at 2 to 8°C. Antibody is stable for 24 months.,Non-hazardous. No MSDS required.
Supplied as
200ug/ml of Ab purified from Bioreactor Concentrate by Protein A/G. Prepared in 10mM PBS with 0.05% BSA & 0.05% azide. Also available WITHOUT BSA at 1.0mg/ml.
Limitations
This antibody is available for research use only and is not approved for use in diagnosis.

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Other Information

Functions
  • Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 (PubMed:24012426, PubMed:26865365, PubMed:24318877). Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation (PubMed:27708256). Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle (PubMed:27137183). Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling (PubMed:24613385). Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223).
  • (Microbial infection) In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell.
Key References
  • Toft, D.O., et al. Biochemistry 24.23 (1985 Nov 5): 6586-91.
PubMed Links
Warranty
There are no warranties, expressed or implied, which extend beyond this description. Company is not liable for any personal injury or economic loss resulting from this product.
Entrez Gene ID
3304
SwissProt
P0DMV9Human
Chromosome Location
6p21.33
Mol. Weight of Antigen
70kDa
Alternate Names
Heat shock 70 kDa protein 1B, Heat shock 70 kDa protein 2, Heat shock 70 kDa protein 2; HSP70-2

Summary

This intronless gene encodes a 70kDa heat shock protein which is a member of the heat shock protein 70 family. In conjuction with other heat shock proteins, this protein stabilizes existing proteins against aggregation and mediates the folding of newly translated proteins in the cytosol and in organelles. It is also involved in the ubiquitin-proteasome pathway through interaction with the AU-rich element RNA-binding protein 1.The gene is located in the major histocompatibility complex class III region, in a cluster with two closely related genes which encode similar proteins. [provided by RefSeq]

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