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1000 results found for “Myoglobin”
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Name :
GNG12 HumanDescription:
Guanine Nucleotide Binding Protein Gamma 12 Human Recombinant
Guanine Nucleotide Binding Protein (G Protein), Gamma 12, Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12.
Product # :
PRO-2184Price :
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Shipped with Ice Packs
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Description
GNG12 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 92 amino acids (1-69 a.a) and having a molecular mass of 10.1kDa. GNG12 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GNG12 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Guanine Nucleotide Binding Protein Gamma 12, also known as GNG12 belongs to the Guanine nucleotide-binding proteins (G proteins) which are involved as a modulator or transducer in a variety of transmembrane signaling systems. In addition, the beta as well as gamma chains are essential for the GTPase activity, for replacement of GDP by GTP, and also for G protein-effector interaction.
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Synonyms
Guanine Nucleotide Binding Protein (G Protein), Gamma 12, Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSSKTAS TNNIAQARRT VQQLRLEASI ERIKVSKASA DLMSYCEEHA RSDPLLIGIP TSENPFKDKK TC.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CHMP2B HumanDescription:
Chromatin Modifying Protein 2B Human Recombinant
Chromatin modifying protein 2B, CHMP2.5, VPS2B, Vacuolar protein sorting-associated protein 2-2, hVps2-2, DMT1, DKFZp564O123, VPS2 homolog B.
Product # :
PRO-877Price :
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Description
CHMP2B Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (1-213) and having a molecular mass of 26.1 kDa.The CHMP2B is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CHMP2B protein 1mg/ml is supplied in 20mM Tris-HCL, pH-8, 0.1M NaCl, 2mM DTT and 20% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
CHMP2B is a member of the vacuolar sorting protein family. CHMP2B is a component of the ESCRT-III complex which is essential for sorting endosomal articles into multivesicular bodies (MVBs), and are also obligatory for the formation of these bodies. CHMP2B is usually found in brain, heart, skeletal muscle, small intestine, pancreas, lung, placenta and leukocytes.
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Synonyms
Chromatin modifying protein 2B, CHMP2.5, VPS2B, Vacuolar protein sorting-associated protein 2-2, hVps2-2, DMT1, DKFZp564O123, VPS2 homolog B.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MASLFKKKTV DDVIKEQNRE LRGTQRAIIR DRAALEKQEK QLELEIKKMA KIGNKEACKV LAKQLVHLRK QKTRTFAVSS KVTSMSTQTK VMNSQMKMAG AMSTTAKTMQ AVNKKMDPQK TLQTMQNFQK ENMKMEMTEE MINDTLDDIF DGSDDEEESQ DIVNQVLDEI GIEISGKMAK APSAARSLPS ASTSKATISD EEIERQLKAL GVD
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GP9 HumanDescription:
Glycoprotein-9 Human Recombinant
Platelet glycoprotein IX, GP-IX, GPIX, Glycoprotein 9, CD42a, Glycoprotein IX (Platelet).
Product # :
PRO-055Price :
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Description
GP9 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 154 amino acids (17-147) and having a molecular mass of 16.8kDa. GP9 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GP9 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2M UREA and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Glycoprotein-9 (GP9) is a small membrane glycoprotein found on the surface of human platelets. GP9 forms a one to one noncovalent complex with glycoprotein Ib, a platelet surface membrane glycoprotein complex which functions as a receptor for von Willebrand factor. The complete receptor complex includes noncovalent association of the alpha and beta subunits with the protein and platelet glycoprotein V. GP9 gene defects cause the Bernard-Soulier syndrome, aka giant platelet disease whose patients have unusually large platelets and have a clinical bleeding tendency.
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Synonyms
Platelet glycoprotein IX, GP-IX, GPIX, Glycoprotein 9, CD42a, Glycoprotein IX (Platelet).
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSTKDCPSP CTCRALETMG LWVDCRGHGL TALPALPART RHLLLANNSL QSVPPGAFDH LPQLQTLDVT QNPWHCDCSL TYLRLWLEDR TPEALLQVRC ASPSLAAHGP LGRLTGYQLG SCGWQLQASW VRPG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GREM1 HumanDescription:
GREM1 Human Recombinant
Gremlin-1 isoform 1, CKTSF1B1, DAND2, DRM, GREMLIN, IHG-2, PIG2, GREM1, Cell proliferation-inducing gene 2 protein, Cysteine knot superfamily 1, BMP antagonist 1, DAN domain family member 2, Down-regulated in Mos-transformed cells protein, Increased in high glucose protein 2.
Product # :
PRO-1359Price :
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Description
GREM1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (25-184) and having a molecular mass of 20.7 kDa. GREM1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GREM1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
GREM1 belongs to the BMP (bone morphogenic protein) antagonist family. Like BMPs, BMP antagonists comprise cystine knots and usually form homo- and heterodimers. The CAN (cerberus and dan) subfamily of BMP antagonists, to which GREM1 belongs, is characterized by a C-terminal cystine knot with an eight-membered ring. The antagonistic effect of the secreted glycosylated protein is because of its direct binding to BMP proteins. As an antagonist of BMP, GREM1 takes a place in regulating organogenesis, body patterning, and tissue differentiation. In mouse, GREM1 has been shown to convey the sonic hedgehog (SHH) signal from the polarizing region to the apical ectodermal ridge during limb bud outgrowth. Alternatively merged transcript variants encoding different isoforms have been found for this gene.
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Synonyms
Gremlin-1 isoform 1, CKTSF1B1, DAND2, DRM, GREMLIN, IHG-2, PIG2, GREM1, Cell proliferation-inducing gene 2 protein, Cysteine knot superfamily 1, BMP antagonist 1, DAN domain family member 2, Down-regulated in Mos-transformed cells protein, Increased in high glucose protein 2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSKKKGSQG AIPPPDKAQH NDSEQTQSPQ QPGSRNRGRG QGRGTAMPGE EVLESSQEAL HVTERKYLKR DWCKTQPLKQ TIHEEGCNSR TIINRFCYGQ CNSFYIPRHI RKEEGSFQSC SFCKPKKFTT MMVTLNCPEL QPPTKKKRVT RVKQCRCISI DLD.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CXCL1 HumanDescription:
GRO-Alpha Human Recombinant (CXCL1)
Growth-regulated protein alpha, CXCL1, Melanoma growth stimulatory activity, MGSA, Neutrophil-activating protein 3, NAP-3, GRO-alpha (1-73), chemokine (C-X-C motif) ligand 1, GRO1, GROa, SCYB1, MGSA-a, MGSA alpha.
Product # :
CHM-329Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
GRO Alpha Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7811 Dalton. The GRO-alpha is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in 20mM PB, pH 7.4, 50mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.
More Info
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Introduction
Chemokine (C-X-C motif) ligand 1 (CXCL1) is a small cytokine belonging to the CXC chemokine family that was previously called GRO1 oncogene, Neutrophil-activating protein 3 (NAP-3) and melanoma growth stimulating activity, alpha (MSGA-a). It is secreted by human melanoma cells, has mitogenic properties and is implicated in melanoma pathogenesis. CXCL1 is expressed by macrophages, neutrophilsand epithelial cells, and has neutrophil chemoattractant activity. CXCL1 plays a role in spinal cord development by inhibiting the migration of oligodendrocyte precursors and is involved in the processes of angiogenesis, inflammation, wound healing, and tumorigenesis. This chemokine elicits its effects by signaling through the chemokine receptor CXCR2. The gene for CXCL1 is located on human chromosome 4 amongst genes for other CXC chemokines.
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Synonyms
Growth-regulated protein alpha, CXCL1, Melanoma growth stimulatory activity, MGSA, Neutrophil-activating protein 3, NAP-3, GRO-alpha (1-73), chemokine (C-X-C motif) ligand 1, GRO1, GROa, SCYB1, MGSA-a, MGSA alpha.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GRO-alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL1 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CXCL1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ser-Val-Ala-Thr.
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Background
What is the molecular weight/Mw of CXCL1 HUMAN Protein?
CXCL1 HUMAN Protein has a total Mw of 7.81kDa.
What is the source or expression system of CXCL1 HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL1 HUMAN Protein?
CXCL1 HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL1 HUMAN Protein?
Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.
What is the amino acid sequence of CXCL1 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ser-Val-Ala-Thr.
What applications can CXCL1 HUMAN Protein be used in?
CXCL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL1 HUMAN Protein?
The endotoxin level is minimal, CXCL1 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GroEL HumanDescription:
GroEL (HSP60) Human Recombinant
CPN60, GROEL, HSP60, HSP65, SPG13, CHA60, GROL, crpA, mopA, 60 kDa heat shock protein mitochondrial, Heat shock protein 60, HSP-60, 60 kDa chaperonin, Chaperonin 60, Mitochondrial matrix protein P1, P60 lymphocyte protein, HuCHA60, HSPD1.
Product # :
HSP-016Price :
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Shipped with Ice Packs
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Description
Recombinant Human GroEL, HSP60 produced in E.Coli is a single, non-glycosylated polypeptide chain fused to a 20 a.a. His tag at N-terminus containing 593 amino acids (1-573 a.a.) and having a molecular mass of 63kDa.The HSP60 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GroEL protein contains 20mM Tris-HCl buffer pH-8.0, 5mM DTT and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
GroEL, HSP60 is a chaperonin located in the mitochondria which is responsible for the transportation & refolding of proteins from the cytoplasm directly into the mitochondrial matrix. GroEL is regulated by the HSP10 cochaperonin, which is a single heptameric protein ring having a molecular mass of 10 kDa which form a unique complex with HSP60. HSP10, GroES coordinates the ATPase activity of the HSP60 subunits in order to allow the release of bound polypeptide in a manner that is productive for its correct folding.
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Synonyms
CPN60, GROEL, HSP60, HSP65, SPG13, CHA60, GROL, crpA, mopA, 60 kDa heat shock protein mitochondrial, Heat shock protein 60, HSP-60, 60 kDa chaperonin, Chaperonin 60, Mitochondrial matrix protein P1, P60 lymphocyte protein, HuCHA60, HSPD1.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MLRLPTVFRQ MRPVSRVLAP HLTRAYAKDV KFGADARALMLQGVDLLADA VAVTMGPKGR TVIIEQSWGS PKVTKDGVTV AKSIDLKDKY KNIGAKLVQDVANNTNEEAG DGTTTATVLA RSIAKEGFEK ISKGANPVEI RRGVMLAVDA VIAELKKQSKPVTTPEEIAQ VATISANGDK EIGNIISDAM KKVGRKGVIT VKDGKTLNDE LEIIEGMKFD RGYISPYFIN TSKGQKCEFQ DAYVLLSEKK ISSIQSIVPA LEIANAHRKP LVIIAEDVDG EALSTLVLNR LKVGLQVVAV KAPGFGDNRK NQLKDMAIAT GGAVFGEEGL TLNLEDVQPH DLGKVGEVIV TKDDAMLLKG KGDKAQIEKR IQEIIEQLDV TTSEYEKEKL NERLAKLSDG VAVLKVGGTS DVEVNEKKDR VTDALNATRA AVEEGIVLGG GCALLRCIPA LDSLTPANED QKIGIEIIKR TLKIPAMTIA KNAGVEGSLI VEKIMQSSSE VGYDAMAGDF VNMVEKGIID PTKVVRTALL DAAGVASLLT TAEVVVTEIP KEEKDPGMGA MGGMGGGMGG GMF.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
UNC119B HumanDescription:
UNC-119 Homolog B Human Recombinant
Unc-119 homolog B (C. elegans), POC7B, POC7 centriolar protein homolog B, MGC5139.
Product # :
PRO-1034Price :
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Shipped with Ice Packs
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Description
UNC119B Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 271 amino acids (1-251) and having a molecular mass of 30.3kDa.UNC119B is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The UNC119B solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
UCN119B is a member of the PDE6D/unc-119 family. UCN119B has a large number of photoreceptors of the retina. Additionaly, UCN119B has a strong homology with the C. elegans unc119 and is able to functionally complement the C. elegans unc119 mutation gene.
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Synonyms
Unc-119 homolog B (C. elegans), POC7B, POC7 centriolar protein homolog B, MGC5139.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSGSNPKAAA AASAAGPGGL VAGKEEKKKA GGGVLNRLKA RRQAPHHAAD DGVGAAVTEQ ELLALDTIRP EHVLRLSRVT ENYLCKPEDN IYSIDFTRFK IRDLETGTVL FEIAKPCVSD QEEDEEEGGG DVDISAGRFV RYQFTPAFLR LRTVGATVEF TVGDKPVSNF RMIERHYFRE HLLKNFDFDF GFCIPSSRNT CEHIYEFPQL SEDVIRLMIE NPYETRSDSF YFVDNKLIMH NKADYAYNGG Q
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CMC4 HumanDescription:
CX9C Motif Containing 4 Human Recombinant
C-X(9)-C Motif Containing 4, C-X(9)-C Motif Containing 4 Homolog, Mature T-Cell Proliferation 1 Neighbor Protein, MTCP1NB, MTCP1, Mature T-Cell Proliferation-1 Type A, Protein P8 MTCP-1, p8MTCP1, MTCP-1 Type A, C6.1B.
Product # :
PRO-1769Price :
Quantity :
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Shipped with Ice Packs
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Description
CMC4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids (1-68 a.a) and having a molecular mass of 10.4kDa.CMC4 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CMC4 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
CMC4 is a downstream 8kDa protein restricts to mitochondria which was identified by participation in some t(X;14) translocations related with mature T-cell proliferations. This region has a compound gene structure, with a common promoter and 5’ exon spliced to two different groups of 3’ exons which encode 2 separate proteins.
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Synonyms
C-X(9)-C Motif Containing 4, C-X(9)-C Motif Containing 4 Homolog, Mature T-Cell Proliferation 1 Neighbor Protein, MTCP1NB, MTCP1, Mature T-Cell Proliferation-1 Type A, Protein P8 MTCP-1, p8MTCP1, MTCP-1 Type A, C6.1B.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSEFMPQKD PCQKQACEIQ KCLQANSYME SKCQAVIQEL RKCCAQYPKG RSVVCSGFEK EEEENLTRKS ASK
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
VAMP8 HumanDescription:
Endobrevin Human Recombinant
VAMP8, VAMP-8, Endobrevin, Vesicle-Associated Membrane Protein 8, EDB.
Product # :
PRO-660Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
VAMP8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 96 amino acids (1-76 a.a.) and having a molecular mass of 10.9 kDa. The VAMP8 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatography techniques.
Source
Escherichia Coli.
Formulation
The VAMP8 protein solution (0.25mg/ml) contains 20mM Tris pH-8, 0.1mM PMSF, 0.2M NaCl and 50% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
VAMP8 also called endobrevin, is the main component of a SNARE complex involved in the docking and fusion of synaptic vesicles with the presynaptic membrane. VAMP8 protein is involved in the regulatation of enzyme secretion in pancreatic acinar cells and plays a part in the abscission of the midbody during cell division, which leads to completely separate daughter cells. VAMP8 is essential for dense-granule secretion in platelets. VAMP8 is related with the perinuclear vesicular structures of the early endocytic compartment. VAMP8 interacts particularly with the soluble NSF-attachment protein (alpha-SNAP), through an VAMP8-containing SNARE complex.
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Synonyms
VAMP8, VAMP-8, Endobrevin, Vesicle-Associated Membrane Protein 8, EDB.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MEEASEGGGN DRVRNLQSEV EGVKNIMTQN VERILARGEN LEHLRNKTED LEATSEHFKT TSQKVARKFW WKNVKM.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
RAC1 Human, HisDescription:
Ras-Related C3 Botulinum Toxin substrate 1 Human Recombinant, His Tag
P21-RAC1, RAC-1, RAC1, RAS-like protein TC25, MIG5, Cell-migration-inducing gene 5 protein,Ras-related C3 botulinum toxin substrate 1, rho family small GTP binding protein Rac1, TC-25, MGC111543.
Product # :
PRO-731Price :
Quantity :
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Shipped with Ice Packs
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Description
Ras-Related C3 Botulinum Toxin substrate 1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-192 a.a.) and having a molecular mass of 23.6 kDa. RAC1 contains a 20 amino acid His Tag at N-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RAC1 His Tag protein solution contains 20mM Tris-HCl pH7.5, 1mM EDTA, 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
RAC1 is a GTPase which belongs to the RAS superfamily of small GTP-binding proteins. Members of this superfamily appear to regulate a diverse array of cellular events, including the control of cell growth, cytoskeletal reorganization, and the activation of protein kinases. RAC-1 regulates the actin cytoskeleton but also other cellular processes. RAC1 have been shown to be involved in the regulation of cell-cell adhesion.
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Synonyms
P21-RAC1, RAC-1, RAC1, RAS-like protein TC25, MIG5, Cell-migration-inducing gene 5 protein,Ras-related C3 botulinum toxin substrate 1, rho family small GTP binding protein Rac1, TC-25, MGC111543.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP VNLGLWDTAG QEDYDRLRPLSYPQTDVFLI CFSLVSPASF ENVRAKWYPE VRHHCPNTPI ILVGTKLDLR DDKDTIEKLK EKKLTPITYP QGLAMAKEIG AVKYLECSALTQRGLKTVFD EAIRAVLCPP PVKKRKRKCL LL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MCP 1 Human, HisDescription:
Monocyte Chemotactic Protein-1 Human Recombinant (CCL2), His Tag
Small inducible cytokine A2, CCL2, Monocyte chemotactic protein 1, MCP-1, Monocyte chemoattractant protein 1, Monocyte chemotactic and activating factor, MCAF, Monocyte secretory protein JE, HC11, chemokine (C-C motif) ligand 2, MCP1, SCYA2, GDCF-2, SMC-CF, HSMCR30, MGC9434, GDCF-2 HC11.
Product # :
CHM-246Price :
Quantity :
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Shipped with Ice Packs
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Description
MCP-1 Human Recombinant also known as Monocyte Chemotactic and Activating Factor (MCAF) produced in E.Coli is a non-glycosylated, Polypeptide chain containing 97 amino acids (24-99) and having a molecular mass of 10.9 kDa. The MCP-1 is fused to 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The His Tag MCP-1 protein (1mg/ml) solution contains 20mM Tris-HCL pH-8.0, 1mM DTT and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Chemokine (C-C motif) ligand 2 (CCL2) is a small cytokine belonging to the CC chemokine family that is also known as monocyte chemotactic protein-1 (MCP-1). It is found at the site of tooth eruption and bone degradation. In the bone, CCL2 is expressed by mature osteoclasts and osteoblasts and is under the control of nuclear factor ?B (NF?B). CCL2 recruits immune cells, such as monocytes, to sites of tissue injury and infection. This chemokine is produced as a protein precursor containing signal peptide of 23 amino acids and a mature peptide of 76 amino acids. It is a monomeric polypeptide, with a molecular weight of approximately 13kDa. As with many other CC chemokines, CCL2 is located on chromosome 17 in humans. The cell surface receptors that bind CCL2 are CCR2 and CCR5.
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Synonyms
Small inducible cytokine A2, CCL2, Monocyte chemotactic protein 1, MCP-1, Monocyte chemoattractant protein 1, Monocyte chemotactic and activating factor, MCAF, Monocyte secretory protein JE, HC11, chemokine (C-C motif) ligand 2, MCP1, SCYA2, GDCF-2, SMC-CF, HSMCR30, MGC9434, GDCF-2 HC11.
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Physical Appearance
Sterile Filtered colorless clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQPDAINAPV TCCYNFTNRK ISVQRLASYR RITSSKCPKE AVIFKTIVAK EICADPKQKW VQDSMDHLDK QTQTPKT.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CCL12 MouseDescription:
Monocyte Chemotactic Protein-5 Mouse Recombinant (CCL12)
C-C motif chemokine 12, MCP-1-related chemokine, Monocyte chemoattractant protein 5, Monocyte chemotactic protein 5, MCP-5, Small-inducible cytokine A12, Ccl12, Mcp5, Scya12.
Product # :
CHM-266Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
MCP-5 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 82 amino acids and having a molecular mass of 9.3kDa. The MCP5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human peripheral blood monocytes using a concentration range of 10.0-50.0 ng/ml.More Info
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Introduction
MCP-5 (CCL12) is a cloned mouse CC chemokine most closely related to human MCP1 (66% amino acid sequence identity in the mature protein). MCP5 is expressed constitutively in the thymus and the lymph nodes. Under inflammatory conditions, moreover CCL12 expression is induced in activated macrophages and mast cells. The mouse MCP1 gene is mapped to the CC chemokine cluster on chromosome 11. Recombinant CCL12 is a potent chemoattractant for monocytes and lymphocytes but not neutrophils. At high concentrations, MCP-5 also chemoattracts eosinophils. CCL12 is a functional ligand for CCR2.
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Synonyms
C-C motif chemokine 12, MCP-1-related chemokine, Monocyte chemoattractant protein 5, Monocyte chemotactic protein 5, MCP-5, Small-inducible cytokine A12, Ccl12, Mcp5, Scya12.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CCL12 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCP5 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized MCP5 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
GPDAVSTPVT CCYNVVKQKI HVRKLKSYRR ITSSQCPREA VIFRTILDKE ICADPKEKWV KNSINHLDKT SQTFILEPSC LG.
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Background
What is the molecular weight/Mw of CCL12 MOUSE Protein?
CCL12 MOUSE Protein has a total Mw of 9.3kDa.
What is the source or expression system of CCL12 MOUSE Protein?
Escherichia Coli.
What is the Purity of CCL12 MOUSE Protein?
CCL12 MOUSE Protein is > 97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL12 MOUSE Protein?
Determined by its ability to chemoattract human peripheral blood monocytes using a concentration range of 10.0-50.0 ng/ml.
What is the amino acid sequence of CCL12 MOUSE Protein?
GPDAVSTPVT CCYNVVKQKI HVRKLKSYRR ITSSQCPREA VIFRTILDKE ICADPKEKWV KNSINHLDKT SQTFILEPSC LG.
What applications can CCL12 MOUSE Protein be used in?
CCL12 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL12 MOUSE Protein?
The endotoxin level is minimal, CCL12 MOUSE Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
MEIS3 HumanDescription:
Meis Homeobox 3 Human Recombinant
Meis Homeobox 3, Meis1-Related Protein 2, MRG2, Meis1, Myeloid Ecotropic Viral Integration Site 1 Homolog 3 (Mouse), Meis1, Myeloid Ecotropic Viral Integration Site 1 Homolog 3, Homeobox Protein Meis3, Homeobox protein Meis3.
Product # :
PRO-2121Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
MEIS3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 381 amino acids (1-358 a.a) and having a molecular mass of 41.4kDa. MEIS3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MEIS3 protein solution (1 mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Meis Homeobox 3, also known as MEIS3 is a member of the TALE/MEIS homeobox family. MEIS3 contains 1 homeobox DNA-binding domain. In addition, MEIS3 is over expressed in the Brain - Amygdala , Uterus , Brain - Anterior cingulate cortex and Brain – Cortex.
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Synonyms
Meis Homeobox 3, Meis1-Related Protein 2, MRG2, Meis1, Myeloid Ecotropic Viral Integration Site 1 Homolog 3 (Mouse), Meis1, Myeloid Ecotropic Viral Integration Site 1 Homolog 3, Homeobox Protein Meis3, Homeobox protein Meis3.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMARRYDE LPHYPGIVDG PAALASFPET VPAVPGPYGP HRPPQPLPPG LDSDGLKREK DEIYGHPLFP LLALVFEKCE LATCSPRDGA GAGLGTPPGG DVCSSDSFNE DIAAFAKQVR SERPLFSSNP ELDNLMIQAI QVLRFHLLEL EKGKMPIDLVIEDRDGGCRE DFEDYPASCP SLPDQNNMWI RDHEDSGSVH LGTPGPSSGG LASQSGDNSS DQGDGLDTSV ASPSSGGEDE DLDQERRRNK KRGIFPKVAT NIMRAWLFQH LSHPYPSEEQ KKQLAQDTGL TILQVNNWFI NARRRIVQPM IDQSNRTGQG AAFSPEGQPI GGYTETQPHVAVRPPGSVGM SLNLEGEWHY L
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CPOX HumanDescription:
Coproporphyrinogen Oxidase Human Recombinant
CPO, CPX, HCP, Coproporphyrinogen-III oxidase, mitochondrial, COX, Coprogen oxidase, Coproporphyrinogenase, CPOX.
Product # :
ENZ-701Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
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Description
CPOX Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 367 amino acids (111-454) and having a molecular mass of 41.6kDa. CPOX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CPOX solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
Coproporphyrinogen Oxidase (CPOX) which is localized to the internal membrane space of erythrocytes takes part in the 6th phase of heme biosynthesis. CPOX catalyzes the oxidative decarboxylation of propionic acid side chains of rings A and B of coproporphyrinogen III. Mutations in human CPOX gene forecast the clinical result of the disease, with either hepatic hereditary coproporphyria or hematological manifestations of erythropoietic harderoporphyria.
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Synonyms
CPO, CPX, HCP, Coproporphyrinogen-III oxidase, mitochondrial, COX, Coprogen oxidase, Coproporphyrinogenase, CPOX.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSTSLGRPE EEEDELAHRC SSFMAPPVTD LGELRRRPGD MKTKMELLIL ETQAQVCQAL AQVDGGANFS VDRWERKEGG GGISCVLQDG CVFEKAGVSI SVVHGNLSEE AAKQMRSRGK VLKTKDGKLP FCAMGVSSVI HPKNPHAPTI HFNYRYFEVE EADGNKQWWF GGGCDLTPTY LNQEDAVHFH RTLKEACDQH GPDLYPKFKK WCDDYFFIAH RGERRGIGGI FFDDLDSPSK EEVFRFVQSC ARAVVPSYIP LVKKHCDDSF TPQEKLWQQL RRGRYVEFNL LYDRGTKFGL FTPGSRIESI LMSLPLTARW EYMHSPSENS KEAEILEVLR HPRDWVR.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
WWC1 HumanDescription:
WW And C2 Domain Containing 1 Human Recombinant
WW and C2 domain containing 1, HBEBP3, HBEBP36, KIBRA, Protein KIBRA, HBeAg-binding protein 3, Kidney and brain protein, WW domain-containing protein 1, WWC1, KIAA0869.
Product # :
PRO-1863Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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- formulation
- purity
- More Info
Description
WWC1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 152 amino acids (655-783) and having a molecular mass of 17kDa. WWC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The WWC1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
WW and C2 Domain Containing 1 (WWC1) is a cytoplasmic phosphoprotein which interacts with PRKC-zeta and dynein light chain-1. WWC1 takes part in cognition and memory performance. In some individuals, alleles of WWC1 have enhanced memory.
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Synonyms
WW and C2 domain containing 1, HBEBP3, HBEBP36, KIBRA, Protein KIBRA, HBeAg-binding protein 3, Kidney and brain protein, WW domain-containing protein 1, WWC1, KIAA0869.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSEAVGATR IQIALKYDEK NKQFAILIIQ LSNLSALLQQ QDQKVNIRVA VLPCSESTTC LFRTRPLDAS DTLVFNEVFW VSMSYPALHQ KTLRVDVCTT DRSHLEECLG GAQISLAEVC RSGERSTRWY NL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CREG1 MouseDescription:
Cellular Repressor of E1A-Stimulated Genes 1 Mouse Recombinant
Protein CREG1, Cellular repressor of E1A-stimulated genes 1, Creg1, Creg.
Product # :
PRO-2387Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CREG1 Mouse Recombinant produced in E. coli is a single polypeptide chain containing 213 amino acids (32-220) and having a molecular mass of 24kDa. CREG1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CREG1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.15M NaCl.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
Cellular Repressor of E1A-Stimulated Genes 1 (CREG1) both activates and inhibits gene expression to stimulate cellular proliferation and hinder differentiation. CREG1 antagonizes transcriptional activation and cellular transformation by E1A. CREG1 shares partial sequence similarity with E1A and binds both the general transcription factor TBP and the tumor suppressor pRb in vitro. CREG1 contributes to the transcriptional control of cell growth and differentiation.
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Synonyms
Protein CREG1, Cellular repressor of E1A-stimulated genes 1, Creg1, Creg.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMRGGRDH GDWDVDRRLP PLPPREDGPR VARFVTHVSD WGSLATISTI KEVRGWPFAD IISISDGPPG EGTGEPYMYL SPLQQAVSDL QENPEATLTM SLAQTVYCRN HGFDPQSPLC VHIMMSGTVT KVNKTEEDYA RDSLFVRHPE MKHWPSSHNW FFAKLKISRI WVLDYFGGPK VVTPEEYFNV TLQ.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
XRCC3 HumanDescription:
X-Ray Repair Cross Complementing Protein 3 Human Recombinant
X-ray repair cross complementing protein 3, RAD51-like.
Product # :
PRO-2649Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
XRCC3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 366 amino acids (1-346 a.a.) and having a molecular mass of 40 kDa. XRCC3 is fused to a 20 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The XRCC3 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M urea.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
Recombinant Human X-Ray Repair Cross Complementing Protein 3, also referred to XRCC3, is a member of RecA family and RAD51 subfamily. The protein takes partin homologous recombination to maintain chromosome stability and repair DNA damage. XRCC3functionally complements Chinese hamster irs1SF, a repair-deficient mutant that shows hypersensitivity to a number of different DNA-damaging agents & chromosomally unstable.
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Synonyms
X-ray repair cross complementing protein 3, RAD51-like.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDLDLLDLNP RIIAAIKKAK LKSVKEVLHF SGPDLKRLTN LSSPEVWHLL RTASLHLRGS SILTALQLHQ QKERFPTQHQ RLSLGCPVLD ALLRGGLPLD GITELAGRSS AGKTQLALQL CLAVQFPRQH GGLEAGAVYI CTEDAFPHKR LQQLMAQQPR LRTDVPGELL QKLRFGSQIF IEHVADVDTL LECVNKKVPV LLSRGMARLV VIDSVAAPFR
CEFDSQASAP RARHLQSLGA TLRELSSAFQ SPVLCINQVT EAMEEQGAAH GPLGFWDERV SPALGITWAN QLLVRLLADR LREEEAALGC PARTLRVLSA PHLPPSSCSY TISAEGVRGT PGTQSH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ALDH2 Mouse, ActiveDescription:
Aldehyde Dehydrogenase 2 Mouse Recombinant, Active
Aldehyde dehydrogenase, mitochondrial, AHD-M1, ALDH class 2, ALDH-E2, ALDHI.
Product # :
ENZ-1093Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- biological activity
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Description
ALDH2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 523 amino acids (20-519) and having a molecular mass of 56.8kDa. ALDH2 Mouse is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ALDH2 Mouse protein (0.5mg/ml) is formulated in Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 180 pmol/min/ug, and was obtained by measuring the increase of NADH in absorbance at 340 nm resulting from the reduction of NAD at pH 8.0 at 25C.
More Info
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Introduction
ALDH2 is part of the aldehyde dehydrogenase family of proteins which catalyze the chemical transformation from acetaldehyde to acetic acid. ALDH2 is the second enzyme of the major oxidative pathway of alcohol metabolism. ALDH2 has 2 major liver isoforms: cytosolic and mitochondrial, which differ by their electrophoretic mobilities, kinetic properties, and subcellular localizations. Nearly all Caucasians have 2 major isozymes, whereas roughly 50% of Orientals have only the cytosolic isozyme, omitting the mitochondrial isozyme. The extremely higher rate of acute alcohol intoxication with Orientals compared to Caucasians is due to the fact of the absence of mitochondrial isozyme. ALDH2 has a low Km for acetaldehydes, and is localized in mitochondrial matrix.
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Synonyms
Aldehyde dehydrogenase, mitochondrial, AHD-M1, ALDH class 2, ALDH-E2, ALDHI.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSSAAATSA VPAPNHQPEV FCNQIFINNE WHDAVSRKTF PTVNPSTGEV ICQVAEGNKE DVDKAVKAARAAFQLGSPWR RMDASDRGRL LYRLADLIER DRTYLAALET LDNGKPYVIS YLVDLDMVLK CLRYYAGWAD KYHGKTIPID GDFFSYTRHEPVGVCGQIIP WNFPLLMQAW KLGPALATGN VVVMKVAEQT PLTALYVANL IKEAGFPPGV VNIVPGFGPT AGAAIASHEG VDKVAFTGSTEVGHLIQVAA GSSNLKRVTL ELGGKSPNII MSDADMDWAV EQAHFALFFN QGQCCCAGSR TFVQENVYDE FVERSVARAK SRVVGNPFDSRTEQGPQVDE TQFKKILGYI KSGQQEGAKL LCGGGAAADR GYFIQPTVFG DVKDGMTIAK EEIFGPVMQI LKFKTIEEVV GRANDSKYGLAAAVFTKDLD KANYLSQALQ AGTVWINCYD VFGAQSPFGG YKMSGSGREL GEYGLQAYTE VKTVTVKVPQ KNS.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Protein-G HisDescription:
Protein G His Tag Recombinant
Product # :
PRO-1237Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Protein G His Tag Recombinant produced in E.Coli is a 201 amino acids protein which contains amino acid 190-384 of the Streptococcus sp with a C-terminal 6-His tag, and having a molecular mass of 21.6kDa. But it migrates with an apparent molecular mass of 32kDa in SDS-PAGE.The Protein G His Tag is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized with no additives.
Purity
Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.
More Info
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Protein G although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein G should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Protein G in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Applications
Protein G binds to the constant region of many species of immunoglobulin G. It can be used to detect, quantify and purify IgG antibodies and antibody/antigen complexes. Recombinant Protein G contains only IgG binding domains. The albumin-binding domain as well as cell wall and cell membrane binding domains have been removed to ensure the maximum specific IgG binding capacity.
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Specificity
1. Binds with greater affinity to most mammalian immunoglobulins than Protein A, including human IgG3 and rat IgG2a.2. Does not bind to human IgM, IgD and IgA.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Globular Adiponectin MouseDescription:
Globular Adiponectin Mouse Recombinant
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-432Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
- formulation
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- More Info
- sds-page
Description
The globular domain of Adiponectin Mouse Recombinant / Acrp30 Mouse contains 138 amino acid residues from a.a. 111-247 having molecular mass of 16 kDa was over expressed in E.coli and purified by using conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
Acrp30 Mouse (1mg/ml) solution containing 20mM Tris-HCl pH7.5, 50mM NaCl, 5mM DTT and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Adiponectin (247amino acids) is adipocyte complement-related protein of 30 kDa and exclusively expressed in differentiated adipocytes. APM-1 (Acrp30 Mouse) is a member of the complement factor C1q family and consists of signal sequence, Non-homologous sequence, collagen domain and domain (gAcrp30).
Adiponectin expression is reduced in a variety of obese and insulin-resistant states in human, monkeys and mice. Injection of Acrp30 Mouse (247aa) or gAcrp30 (globular domain) lowers serum glucose and free fatty acid level in mice. -
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MAYMYRSAFS VGLETRVTVP NVPIRFTKIF YNQQNHYDGS TGKFYCNIPG LYYFSYHITVYMKDVKVSLF KKDKAVLFTY DQYQEKNVDQ ASGSVLLHLE VGDQVWLQVY GDGDHNGLYADNVNDSTFTG FLLYHDTN
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Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 16kDa.
What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
The biological functionality of ADIPONECTIN Protein will be determined in the future.
What is the amino acid sequence of ADIPONECTIN Protein?
MAYMYRSAFS VGLETRVTVP NVPIRFTKIF YNQQNHYDGS TGKFYCNIPG LYYFSYHITVYMKDVKVSLF KKDKAVLFTY DQYQEKNVDQ ASGSVLLHLE VGDQVWLQVY GDGDHNGLYADNVNDSTFTG FLLYHDTN
What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN Protein was purified using conventional chromatography techniques..
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Y.Enterocolitica (O:9) YopDDescription:
Yersinia Enterocolitica (O:9) YopD Recombinant
Product # :
PRO-2276Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
- purity
- More Info
Description
Recombinant Yersinia Enterocolitica (O:9) YopD produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 34,603 Dalton. Y.Enterocolitica (O:9) YopD is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Y.Enterocolitica (O:9) YopD is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Yersinia enterocolitica is a Gram-negative bacillus-shaped bacterium, which is a member of the Enterobacteriaceae family. Y.Enterocolitica is motile at temperatures between 22-29°C, however becomes non-motile at normal human body temperature. Y. Enterocolitica infection causes the yersiniosis disease, which is an animal-borne disease occurring in humans, as well as in a various groups of animals such as cattle, deer, pigs, and birds. Yersinia enterocolitica is a heterogeneous group of strains, which are conventionally classified by bio-typing into six bio-groups on the basis of phenotypic characteristics, and by serotyping into more than 57 “O” serogroups, on the basis of their O (lipopolysaccharide or LPS) surface antigen. Five of the six biogroups (1B and 2–5) are considered as pathogens. Nevertheless, only a few of these serogroups have been linked with disease in either humans or animals. Strains which belong to serogroups O:3 (biogroup 4), O:5,27 (biogroups 2 and 3), O:8 (biogroup 1B), and O:9 (biogroup 2) are most frequently isolated worldwide from human samples. Still, the main Y. enterocolitica serogroup in many European countries is serogroup O:3 followed by O:9, whereas the serogroup O:8 is mostly detected in the United States.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG- and IgM- and IgA-type human antibodies.2. Immunodot test with positive/negative sera panels.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
s100bb BovineDescription:
s100bb Bovine homodimer
Product # :
PRO-2796Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
s100bb Bovine is suitable for use as a standard in immunoassay and as an immunogen for antiserum production.
Source
Bovine brain tissue.
Formulation
s100bb was lyophilized from 5mM Tris-HCl, pH 7.5, 2mM EDTA and 5mM 2-mercaptoethanol.
Purity
Greater than 95.0% .
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized s100bb homodimer although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution s100bb should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized s100bb in sterile 18MΩ-cm H2O containing 5mM 2- mercaptoethanol not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
S100BB, a member of the S100 family of proteins, is a calcium-binding protein that plays a significant role in various cellular processes, particularly in the central nervous system (CNS). Initially identified as a brain-specific protein, S100BB has captured the attention of researchers due to its involvement in neurological signaling, brain development, and its potential implications in neurological disorders. This research delves into the enigmatic world of S100BB, aiming to uncover its diverse functions, regulatory mechanisms, and its relevance in health and disease.
Discovery and Structural Insights:
S100BB was first discovered in the brain, primarily localized in astrocytes, a type of glial cell in the CNS. Structurally, S100BB is characterized by its EF-hand motifs, allowing it to bind calcium ions, a property crucial for its function. These calcium-binding abilities enable S100BB to participate in intricate cellular signaling pathways, making it a vital player in the dynamic communication within the CNS.
Neurological Signaling and Plasticity:
Within the CNS, S100BB has been implicated in neuronal signaling and synaptic plasticity. It interacts with several target proteins, modulating their activities and influencing processes like neurotransmitter release and neuronal differentiation. Furthermore, S100BB participates in the regulation of intracellular calcium levels, a key factor in neuronal excitability and synaptic transmission. Understanding these roles is vital for unraveling the complexities of neurological function and plasticity.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
HB-EGF HumanDescription:
HB-EGF Human Recombinant
HBEGF, DTR, DTS, HEGFL, HB-EGF, Diphtheria toxin receptor, DT-R, DTSF.
Product # :
CYT-119Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
HB-EGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 87 amino acids and having a molecular mass of 9.9kDa. The HB-EGF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution containing 10mM sodium phosphate pH-7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 was determined by the ability to induce proliferation of 3T3 cells and is 0.13-0.2ng/ml. This corresponds to an expected specific activity of 7.7 x 106units/mg.
More Info
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Introduction
HB-EGF is an EGF related growth factor which signals via the EGF receptor, and stimulates the proliferation of SMC (smooth muscle cells), fibroblasts, epithelial cells and keratinocytes. HB-EGF is expressed in various cell types and tissues, including vascular endothelial cells and SMC, macrophages, skeletal muscle, keratinocytes and particular tumor cells. HB-EGF’s ability to explicitly bind HPR sulfate proteoglycans is dissimilar from other EGF-like molecules, and might be related to the enhanced mitogenic activity, relative to EGF, that HB-EGF exerts on smooth muscle cells.
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Synonyms
HBEGF, DTR, DTS, HEGFL, HB-EGF, Diphtheria toxin receptor, DT-R, DTSF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Human HB-EGF Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HB-EGF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Human HB-EGF in sterile 18M-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MDLQEADLDL LRVTLSSKPQ ALATPNKEEH GKRKKKGKGL GKKRDPCLRK YKDFCIHGEC
KYVKELRAPS CICHPGYHGE RCHGLSL.
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Background
What is the molecular weight/Mw of HB-EGF Protein?
HB-EGF Protein has a total Mw of 9.9kDa.
What is the source or expression system of HB-EGF Protein?
Escherichia Coli.
What is the Purity of HB-EGF Protein?
HB-EGF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of HB-EGF Protein?
The ED50 was determined by the ability to induce proliferation of 3T3 cells and is 0.13-0.2ng/ml. This corresponds to an expected specific activity of 7.7 x 106units/mg.
What is the amino acid sequence of HB-EGF Protein?
MDLQEADLDL LRVTLSSKPQ ALATPNKEEH GKRKKKGKGL GKKRDPCLRK YKDFCIHGEC
KYVKELRAPS CICHPGYHGE RCHGLSL.
What applications can HB-EGF Protein be used in?
HB-EGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for HB-EGF Protein?
The endotoxin level is minimal, HB-EGF Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CCL13 HumanDescription:
Monocyte Chemotactic Protein-4 Human Recombinant (CCL13)
Small inducible cytokine A13, CCL13, Monocyte chemotactic protein 4, MCP-4, Monocyte chemoattractant protein 4, CK-beta-10, NCC-1, chemokine (C-C motif) ligand 13, NCC1, CKb10, SCYL1, SCYA13, MGC17134.
Product # :
CHM-319Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Monocyte Chemotactic Protein-4 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 75 amino acids and having a molecular mass of 8.6 kDa. The MCP-4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) sterile solution in 20mM PB, pH 7.4, 130mM NaCl.
Purity
Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity as determined by the ability of MCP-4 to chemoattaract human monocytes at 10-100ng/ml, corresponding to a Specific Activity of 10,000-100,000 units/mg.More Info
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Introduction
Chemokine (C-C motif) ligand 13 (CCL13 / MCP-4) is a small cytokine belonging to the CC chemokine family. The MCP-4 gene is located on human chromosome 17 within a large cluster of other CC chemokines. MCP-4 induces chemotaxis in monocytes, eosinophils, T lymphocytes, and basophils by binding cell surface G-protein linked chemokine receptors such as CCR2, CCR3 and CCR5. Activity of the MCP-4 chemokine has been implicated in allergic reactions such as asthma. MCP-4 can be induced by the inflammatory cytokines interleukin-1 and TNF-a.
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Synonyms
Small inducible cytokine A13, CCL13, Monocyte chemotactic protein 4, MCP-4, Monocyte chemoattractant protein 4, CK-beta-10, NCC-1, chemokine (C-C motif) ligand 13, NCC1, CKb10, SCYL1, SCYA13, MGC17134.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MCP-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCP-4 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized MCP-4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
QPDALNVPSTCCFTFSSKKISLQRLKSYVITTSRCPQKAV
IFRTKLGKEICADPKEKWVQNYMKHLGRKAHTLKT. -
Background
What is the molecular weight/Mw of CCL13 HUMAN Protein?
CCL13 HUMAN Protein has a total Mw of 8.6kDa.
What is the source or expression system of CCL13 HUMAN Protein?
Escherichia Coli.
What is the Purity of CCL13 HUMAN Protein?
CCL13 HUMAN Protein is >96% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL13 HUMAN Protein?
The specific activity as determined by the ability of MCP-4 to chemoattaract human monocytes at 10-100ng/ml, corresponding to a Specific Activity of 10,000-100,000 units/mg.
What is the amino acid sequence of CCL13 HUMAN Protein?
QPDALNVPSTCCFTFSSKKISLQRLKSYVITTSRCPQKAV
IFRTKLGKEICADPKEKWVQNYMKHLGRKAHTLKT.
What applications can CCL13 HUMAN Protein be used in?
CCL13 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL13 HUMAN Protein?
The endotoxin level is minimal, CCL13 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.