Skip to main content

🚀 Special Offer🚀Get 25% off on your bioreagent online order (except Micelles and Nanodiscs), with the code: PROTEOSHOP25

📢 New ! Accelerate your Antibody Development with Ready-to-use Stable Cell Pools

Explore Now

A. thaliana HSP17 Recombinant Protein

Reference:
size

100ug, 50ug

Brand

ProteoGenix

Product type

Recombinant Proteins

Host Species

Escherichia coli (E. coli)

Applications

Elisa, WB

Product nameA. thaliana HSP17 Recombinant Protein
Uniprot IDP19036
Uniprot linkhttp://www.uniprot.org/uniprot/P19036
Origin speciesA. thaliana
Expression systemProkaryotic expression
SequenceMAHNHRHKHKLPRAMSLVPSFFGGRRTNVFDPFSLDVWDPFEGFLTPGLTNAPAKDVAAFTNAKVDWRETPEAHVFKADV PGLKKEEVKVEVEDGNILQISGERSSENEEKSDTWHRVERSSGKFMRRFRLPENAKVEEVKASMENGVLSVTVPKVQESK PEVKSVDISG
Molecular weight19,11 kDa
Protein delivered with Tag?Yes
Purity estimated>95%
BufferPBS, imidazole 250mM, Urea 4M, pH 8.0
Formliquid
Delivery conditionDry Ice
Delivery lead time in business days10-25
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
BrandProteoGenix
Host speciesEscherichia coli (E.coli)
Fragment TypeFull-length
Protein AccessionNP_190209.1
Spec:Entrez GeneID823768
Spec:NCBI Gene AliasesARABIDOPSIS THALIANA HEAT SHOCK PROTEIN 17.4, heat shock protein 17.4, SMALL HEAT-SHOCK PROTEIN 17.4, ATHSP17.4
Spec:SwissProtIDP19036
NCBI ReferenceNP_190209.1
Aliases /SynonymsHSP17, heat shock protein 17.4, 17.4 kDa class I heat shock protein, 17.4 kDa heat shock protein 1, AtHsp17.4A
ReferencePX-P1065
NoteFor research use only

Description of A. thaliana HSP17 Recombinant Protein

General information on A. thaliana HSP17 Recombinant Protein:

Recombinant human HSP17, also known as Heat Shock 17.4 kDa class I heat shock protein. Heat shock proteins (HSP) are a family of proteins that are produced by cells in reaction to exposure to stressful environment. They can be expressed during exposure heat shock, to cold, UV light, and during wound healing or tissue remodeling. A lot of members from this group perform chaperone function by stabilizing new proteins to ensure correct folding or by helping to refold proteins that were damaged by the cell stress. This increase in expression is transcriptionally regulated.

Publication

  • 1: Wehmeyer N, Hernandez LD, Finkelstein RR, Vierling E. Synthesis of small_x000D_ heat-shock proteins is part of the developmental program of late seed maturation._x000D_ Plant Physiol. 1996 Oct;112(2):747-57. PubMed PMID: 8883386; PubMed Central_x000D_ PMCID: PMC157999.
  • _x000D_ _x000D_ _x000D_
  • 2: Kim DH, Xu ZY, Na YJ, Yoo YJ, Lee J, Sohn EJ, Hwang I. Small heat shock_x000D_ protein Hsp17.8 functions as an AKR2A cofactor in the targeting of chloroplast_x000D_ outer membrane proteins in Arabidopsis. Plant Physiol. 2011 Sep;157(1):132-46._x000D_ doi: 10.1104/pp.111.178681. Epub 2011 Jul 5. PubMed PMID: 21730198; PubMed_x000D_ Central PMCID: PMC3165864.
  • _x000D_ _x000D_ _x000D_
  • 3: Dortay H, Gruhn N, Pfeifer A, Schwerdtner M, Schmülling T, Heyl A. Toward an_x000D_ interaction map of the two-component signaling pathway of Arabidopsis thaliana. J_x000D_ Proteome Res. 2008 Sep;7(9):3649-60. doi: 10.1021/pr0703831. Epub 2008 Jul 22._x000D_ PubMed PMID: 18642946.
  • _x000D_ _x000D_ _x000D_
  • 4: Salanoubat M, Lemcke K, Rieger M, Ansorge W, Unseld M, Fartmann B, Valle G,_x000D_ Blöcker H, Perez-Alonso M, Obermaier B, Delseny M, Boutry M, Grivell LA, Mache R,_x000D_ Puigdomènech P, De Simone V, Choisne N, Artiguenave F, Robert C, Brottier P,_x000D_ Wincker P, Cattolico L, Weissenbach J, Saurin W, Quétier F, Schäfer M,_x000D_ Müller-Auer S, Gabel C, Fuchs M, Benes V, Wurmbach E, Drzonek H, Erfle H, Jordan _x000D_ N, Bangert S, Wiedelmann R, Kranz H, Voss H, Holland R, Brandt P, Nyakatura G,_x000D_ Vezzi A, D'Angelo M, Pallavicini A, Toppo S, Simionati B, Conrad A, Hornischer K,_x000D_ Kauer G, Löhnert TH, Nordsiek G, Reichelt J, Scharfe M, Schön O, Bargues M, Terol_x000D_ J, Climent J, Navarro P, Collado C, Perez-Perez A, Ottenwälder B, Duchemin D,_x000D_ Cooke R, Laudie M, Berger-Llauro C, Purnelle B, Masuy D, de Haan M, Maarse AC,_x000D_ Alcaraz JP, Cottet A, Casacuberta E, Monfort A, Argiriou A, flores M, Liguori R, _x000D_ Vitale D, Mannhaupt G, Haase D, Schoof H, Rudd S, Zaccaria P, Mewes HW, Mayer KF,_x000D_ Kaul S, Town CD, Koo HL, Tallon LJ, Jenkins J, Rooney T, Rizzo M, Walts A,_x000D_ Utterback T, Fujii CY, Shea TP, Creasy TH, Haas B, Maiti R, Wu D, Peterson J, Van_x000D_ Aken S, Pai G, Militscher J, Sellers P, Gill JE, Feldblyum TV, Preuss D, Lin X,_x000D_ Nierman WC, Salzberg SL, White O, Venter JC, Fraser CM, Kaneko T, Nakamura Y,_x000D_ Sato S, Kato T, Asamizu E, Sasamoto S, Kimura T, Idesawa K, Kawashima K, Kishida _x000D_ Y, Kiyokawa C, Kohara M, Matsumoto M, Matsuno A, Muraki A, Nakayama S, Nakazaki_x000D_ N, Shinpo S, Takeuchi C, Wada T, Watanabe A, Yamada M, Yasuda M, Tabata S;_x000D_ European Union Chromosome 3 Arabidopsis Sequencing Consortium.; Institute for_x000D_ Genomic Research.; Kazusa DNA Research Institute.. Sequence and analysis of_x000D_ chromosome 3 of the plant Arabidopsis thaliana. Nature. 2000 Dec_x000D_ 14;408(6814):820-2. PubMed PMID: 11130713.

Reviews

There are no reviews yet.

REVIEW YOUR PRODUCT

Be the first to review “A. thaliana HSP17 Recombinant Protein”

Your email address will not be published. Required fields are marked *

Contact us

Send us a message from the form below

    Cart (0 Items)

    Your cart is currently empty.

    View Products