You are viewing an incomplete version of our website. Please click to reload the website as full version.

HSP70 antibody (Heat Shock Protein 70) (C-Term)

Details for Product anti-HSP70 Antibody No. ABIN361872, Supplier: Login to see
Antigen
  • HSP70
  • HEAT SHOCK PROTEIN 70
  • HEAT SHOCK PROTEIN 70-7
  • HSC70-7
  • K9P8.5
  • K9P8_5
  • chloroplast heat shock protein 70-2
  • cpHsc70-2
  • F19K16.12
  • F19K16_12
  • LOC100305036
  • hsc70
  • CG31354
  • Hsp70Bb
  • hsp70B
  • hsp70Bb-prime
  • DmelCG5834
  • CG5834
  • APG-2
  • HS24/P52
  • HSPH2
  • RY
  • hsp70
  • hsp70RY
  • hsc71
  • Hsp70
  • Hsp70-1
  • Hsp70.1
  • hsp68
  • Hsp110
  • irp94
  • HSPA1
  • HSP70B'
  • HSPA6
  • ARABIDOPSIS HEAT SHOCK PROTEIN 70
  • ATHSP70
  • heat shock protein 70
  • hsp70-5
Epitope
C-Term
55
36
34
26
17
15
13
13
12
4
4
3
3
2
2
2
2
2
2
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
Reactivity
Chlamydomonas reinhardtii (C. reinhardtii)
556
256
255
110
110
97
94
70
62
59
58
57
53
48
47
40
38
35
35
25
24
22
20
18
18
18
8
6
5
4
4
4
4
3
3
3
3
3
3
2
2
2
2
2
1
1
1
1
1
1
1
1
1
1
Host
Rabbit
360
294
40
18
Clonality
Polyclonal
Conjugate
This HSP70 antibody is un-conjugated
32
32
24
21
21
19
19
19
19
19
19
19
19
19
19
19
17
7
6
5
5
5
5
5
5
5
2
1
1
1
Application
Immunoprecipitation (IP), Western Blotting (WB)
623
276
253
251
239
220
91
82
55
52
27
18
12
9
3
2
2
1
1
1
Supplier
Login to see
Supplier Product No.
Login to see
Request

Showcase your results, aid the scientific community, and receive a full refund.

Contribute a validation

Learn more

Immunogen Mature HSP70B protein expressed with N- and C- terminal hexahistidine tags in E.coli, purified with Ni-NTA
Specificity Detects ~70 kDa.
Purification Rabbit antiserum
Alternative Name HSP70 (HSP70 Antibody Abstract)
Background HSP70B (heat shock protein 70B) is a nuclear-encoded, chloroplast-targeted chaperone of the HSP70 family. It is the major HSP70 in the stroma of Chlamydomonas chloroplasts. It interacts with HSP90C, CGE1, CDJ2 and VIPP1 (1-3). It has been shown that using Chlamydomonas reinhardtii as plant model organism the alga encodes a HEP homolog (termed HEP2) that is localized to the stroma (4). HEP2 is expressed constitutively as a low abundance protein with an apparent molecular mass of ~21 kDa. In cell extracts HEP2 interacts with HSP70B in an ATP-dependent fashion. Coexpression of HSP70B with HEP2 in E. coli yields high levels of CGE1- binding competent HSP70B, which also displayed ATPase activity (4). Inactive HSP70B was more prone to proteolysis than active HSP70B. Although inactive HSP70B interacts with HEP2, it is not activated. Active HSP70B remains active for 48 h in the absence of HEP2, suggesting that HEP2 was not involved in maintaining HSP70B in an active state. However, it was found that some HSP70B expressed as a fusion protein with an N-terminal extension was activated when HEP2 was present during cleavage of the fusion protein, suggesting that in vivo HEP2 might be required for renewed folding of HSP70B after transit peptide cleavage (4).
Cellular Localization: Cytoplasm
Gene ID 5722220
NCBI Accession XP_001696432
UniProt A8HYV3
Research Area Heat Shock Proteins
Pathways
Application Notes Recommended Dilution: WB (1:10000)
Optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Lyophilized
Storage -20 °C
Background publications Willmund, Hinnenberger, Nick et al.: "Assistance for a chaperone: Chlamydomonas HEP2 activates plastidic HSP70B for cochaperone binding." in: The Journal of biological chemistry, Vol. 283, Issue 24, pp. 16363-73, 2008 (PubMed).

Liu, Willmund, Whitelegge et al.: "J-domain protein CDJ2 and HSP70B are a plastidic chaperone pair that interacts with vesicle-inducing protein in plastids 1." in: Molecular biology of the cell, Vol. 16, Issue 3, pp. 1165-77, 2005 (PubMed).

Schroda, Vallon, Whitelegge et al.: "The chloroplastic GrpE homolog of Chlamydomonas: two isoforms generated by differential splicing." in: The Plant cell, Vol. 13, Issue 12, pp. 2823-39, 2001 (PubMed).

Schroda, Vallon, Wollman et al.: "A chloroplast-targeted heat shock protein 70 (HSP70) contributes to the photoprotection and repair of photosystem II during and after photoinhibition." in: The Plant cell, Vol. 11, Issue 6, pp. 1165-78, 1999 (PubMed).