HSP70-1A (HSPA1A) Rabbit Polyclonal Antibody

CAT#: TA332380

Rabbit anti-HSPA1A Polyclonal Antibody


USD 275.00

3 Weeks*

Size
    • 100 ul

Product Images

Frequently bought together (3)
Recombinant protein of human heat shock 70kDa protein 1A (HSPA1A)
    • 20 ug

USD 823.00


Transient overexpression lysate of heat shock 70kDa protein 1A (HSPA1A)
    • 100 ug

USD 396.00


beta Actin Mouse Monoclonal Antibody, Clone OTI1, Loading Control
    • 30 ul

USD 159.00

Other products for "HSPA1A"

Specifications

Product Data
Applications IF, WB
Recommended Dilution WB 1:500 - 1:2000
Reactivities Human, Mouse
Host Rabbit
Isotype IgG
Clonality Polyclonal
Immunogen N term –peptide of human HSPA1A
Formulation Store at -20°C (regular) and -80°C (long term). Avoid freeze / thaw cycles. Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.
Concentration lot specific
Purification Affinity purification
Conjugation Unconjugated
Storage Store at -20°C as received.
Stability Stable for 12 months from date of receipt.
Predicted Protein Size 641
Gene Name heat shock protein family A (Hsp70) member 1A
Background HSPA1A and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress (1). Both HSPA1A and HSP90 are able to interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP- and co-chaperone-dependent manner (1). HSPA1A has a broad range of substrates including newly synthesized and denatured proteins, while HSP90 tends to have a more limited subset of substrates, most of which are signaling molecules. HSPA1A and HSP90 often function collaboratively in a multi-chaperone system, which requires a minimal set of co-chaperones: HSP40, Hop, and p23 (2,3). The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments (1,4). When the ubiquitin ligase CHIP associates with the HSPA1A/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome (4). The biological functions of HSPA1A/HSP90 extend beyond their chaperone activity. They are essential for the maturation and inactivation of nuclear hormones and other signaling molecules (1,3). They also play a role in vesicle formation and protein trafficking (2).
Synonyms HEL-S-103; HSP70-1; HSP70-1A; HSP70.1; HSP70I; HSP72; HSPA1
Reference Data
Protein Pathways Antigen processing and presentation, Endocytosis, MAPK signaling pathway, Prion diseases, Spliceosome

{0} Product Review(s)

0 Product Review(s) Submit review

Be the first one to submit a review

Product Citations

*Delivery time may vary from web posted schedule. Occasional delays may occur due to unforeseen complexities in the preparation of your product. International customers may expect an additional 1-2 weeks in shipping.