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1000 results found for “Calumenin”
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Name :
GULP1 HumanDescription:
GULP1 Human Recombinant
GULP, Engulfment Adaptor PTB Domain Containing 1, PTB Domain Adapter Protein CED-6, Cell Death Protein 6 Homolog, CED6, GULP, PTB Domain Adaptor Protein CED-6 Engulfment Adapter Protein, Protein GULP, CED-6.
Product # :
PRO-1398Price :
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Shipped with Ice Packs
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Description
GULP1 Human Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 327 amino acids (1-304a.a) and having a molecular mass of 36.9kDa.GULP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GULP1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 50% glycerol and 2mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
PTB domain-containing engulfment adapter protein 1 (GULP1) is an evolutionarily conserved adaptor protein essential for efficient phagocytosis of apoptotic cells by phagocytes. Furthermore, GULP1 helps modulate cellular glycosphingolipid and cholesterol transport. In addition, GULP1 may have a role in the internalization and endosomal trafficking of various LRP1 ligands, such as PSAP. Increased cytoplasmic levels of GULP1 are linked with increases in cellular levels of GTP-bound ARF6.
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Synonyms
GULP, Engulfment Adaptor PTB Domain Containing 1, PTB Domain Adapter Protein CED-6, Cell Death Protein 6 Homolog, CED6, GULP, PTB Domain Adaptor Protein CED-6 Engulfment Adapter Protein, Protein GULP, CED-6.
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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 MGSMNRAFSR KKDKTWMHTP EALSKHFIPY NAKFLGSTEV EQPKGTEVVR DAVRKLKFAR HIKKSEGQKI PKVELQISIY GVKILEPKTK EVQHNCQLHR ISFCADDKTD KRIFTFICKD SESNKHLCYV FDSEKCAEEI TLTIGQAFDL AYRKFLESGG KDVETRKQIA GLQKRIQDLE TENMELKNKV QDLENQLRIT QVSAPPAGSM TPKSPSTDIF DMIPFSPISH QSSMPTRNGT QPPPVPSRST EIKRDLFGAE PFDPFNCGAA DFPPDIQSKL DEMQEGFKMG LTLEGTVFCL DPLDSRC.
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 :
RELM a MouseDescription:
RELM-alpha Mouse Recombinant
Resistin-like alpha, RELMalpha, Cysteine-rich secreted protein FIZZ1, Parasite-induced macrophage novel gene 1 protein, Cysteine-rich secreted protein A12-gamma, RELM-a.
Product # :
CYT-309Price :
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Shipped at Room temp
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Description
Mouse RELM-alpha Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 88 amino acids and having a molecular mass of 10 kDa. The Mouse RELM-alpha is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Sterile filtered and lyophilized from 0.5mg/ml in 10mM sodium phosphate buffer, pH 7.5.
Purity
Greater than 98% as determined by SDS-PAGE & RP-HPLC.
Citations
More Info
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Introduction
Bronchoalveolar lavage fluid from mice with experimentally induced allergic pulmonary inflammation contains a novel 9.4 kDa cysteine-rich secreted protein, RELM-alpha (FIZZ1, found in inflammatory zone). RELM-alpha is a secreted protein that has a restricted tissue distribution with highest levels in adipose tissue stroma. Murine RELM-alpha (FIZZ1) is the founding member of a new gene family including two other murine genes expressed, respectively, in intestinal crypt epithelium (RELM-beta) and white adipose tissue (Resistin), and two related human genes.
RELMalpha inhibits the differentiation of 3T3-L1 preadipocytes into adipocytes but has no effect on proliferation of 3T3-L1 preadipocytes. RELMalpha is able to form heterooligomers with resistin but not RELMbeta. Since RELMalpha is expressed by adipose tissue and it is a secreted factor, our findings suggest that RELMalpha may be involved in the control of the adipogenesis as well as in the process of muscle differentiation.
In the lung, RELM-alpha is induced by hypoxia and was renamed as hypoxia-induced mitogenic factor (HIMF). HIMF strongly activated Akt phosphorylation. The phosphatidylinositol 3-kinase (PI3K) inhibitor LY294002 (10 micromol/L) inhibited HIMF-activated Akt phosphorylation. It also inhibited HIMF stimulated RPSM proliferation. Thus, the PI3K/Akt pathway, at least in part, mediates the proliferative effect of HIMF. Further studies showed that HIMF had angiogenic and vasoconstrictive properties. HIMF increased pulmonary arterial pressure and vascular resistance. Further studies suggest that HIMF regulates apoptosis and may participate in lung alveolarization and maturation. -
Synonyms
Resistin-like alpha, RELMalpha, Cysteine-rich secreted protein FIZZ1, Parasite-induced macrophage novel gene 1 protein, Cysteine-rich secreted protein A12-gamma, RELM-a.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
At 0.1mg/ml of deionized sterile water.
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Amino Acid Sequence
MDETIEIIVE NKVKELLANP ANYPSTVTKT LSCTSVKTMN RWASCPAGMT ATGCACGFAC GSWEIQSGDT CNCLCLLVDW TTARCCQLS.
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 :
RNF7 HumanDescription:
Ring Finger Protein 7 Human Recombinant
RING-box protein 2 isoform 1, Ring finger protein 7, CKBBP1, ROC2, SAG, RING-box protein 2, Rbx2, CKII beta-binding protein 1, Regulator of cullins 2, Sensitive to apoptosis gene protein, RBX2, RNF7.
Product # :
PRO-1671Price :
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Description
RNF7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 136 amino acids (1-113 a.a) and having a molecular mass of 15.1kDa.RNF7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RNF7 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Ring Finger Protein 7, also known as RNF7, is an extremely conserved ring finger protein. RNF7 is a vital subunit of SKP1-cullin/CDC53-F box protein ubiquitin ligases that are a part of the protein degradation machinery important for cell cycle progression and signal transduction. RNF7 is a substrate of casein kinase II (CSNK2A1/CKII) and also interacts with it. The phosphorylation of RNF7 by CSNK2A1 promotes the degradation of IkappaBalpha (CHUK/IKK-alpha/IKBKA) and p27Kip1(CDKN1B).
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Synonyms
RING-box protein 2 isoform 1, Ring finger protein 7, CKBBP1, ROC2, SAG, RING-box protein 2, Rbx2, CKII beta-binding protein 1, Regulator of cullins 2, Sensitive to apoptosis gene protein, RBX2, RNF7.
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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 MGSMADVEDG EETCALASHS GSSGSKSGGD KMFSLKKWNA VAMWSWDVEC DTCAICRVQV MDACLRCQAE NKQEDCVVVW GECNHSFHNC CMSLWVKQNN RCPLCQQDWV VQRIGK.
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 :
CTF1 RatDescription:
Cardiotrophin-1 Rat Recombinant
Cardiotrophin-1, CT-1, Ctf1.
Product # :
CYT-199Price :
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Shipped at Room temp
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Description
Cardiotrophin-1 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 203 amino acids and having a molecular mass of 21.4kDa.The CTF1 Rat is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.
Biological Activity
The ED50 as determined by the dose-dependent proliferation of TF-1 cells was found to be < 0.5ng/ml, corresponding to a specific activity of > 2.0×106 units/mg.Citations
More Info
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Introduction
Cardiotrophin 1 (CT-1) is a 201 amino acid member of the interleukin-6 superfamily. It was identified by its ability to induce hypertrophic response in cardiac myocytes. CT-1 mRNA levels were found both in cardiac myocytes and in cardiac nonmyocytes. CT 1 was also detected in abundance in normal adult human lung and was expressed in both fetal and adult airway smooth muscle cells. CT 1 activates gp130 dependent signaling and stimulates the Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway to transduce hypertrophic and cytoprotective signals in cardiac myocytes.
CT 1 has also a neurotrophic function. CTF1 deficiency causes increased motoneuron cell death in spinal cord and brainstem nuclei of mice during a period between embryonic day 14 and the first postnatal week. Moreover, CT-1 is a hepatocyte survival factor that efficiently reduces hepatocellular damage in animal models of acute liver injury. Cardiotrophin 1 expression is augmented after hypoxic stimulation and it can protect cardiac cells when added either prior to simulated ischaemia or at the time of reoxygenation following simulated ischaemia. Cardiotrophin 1 can induce expression of the protective heat shock proteins (hsps) in cardiac cells.
Cardiotrophin-1 increased ventricular expression of ANP, brain natriuretic peptide (BNP) and angiotensinogen mRNA.
Cardiophin 1 levels were significantly elevated in patients with heart failure, patients with dilatative cardiomyopathy, moderate/severe mitral regurgitation, stable and unstable angina and after acute myocardial infarction. -
Synonyms
Cardiotrophin-1, CT-1, Ctf1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Cardiotrophin-1 Rat although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CTF1 Rat 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 CTF1 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MSQREGSLED HQTDSSFSFL PHLEAKIRQT HNLARLLTKY ADQLLEEYVQ QQGEPFGLPG FSPPRLPLAG LSGPAPSHAG LPVSERLRQD AAALSALPAL LDAVRRRQAE LNPRAPRLLR SLEDAARQVR ALGAAVETVL AALGAAARGP VPEPVATSAL FTSNSAAGVF SAKVLGLHVC GLYGEWVSRT EGDLGQLVPG GVA.
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Background
What is the molecular weight/Mw of CTF1 Protein?
CTF1 Protein has a total Mw of 21.4kDa.
What is the source or expression system of CTF1 Protein?
Escherichia Coli.
What is the Purity of CTF1 Protein?
CTF1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CTF1 Protein?
The ED50 as determined by the dose-dependent proliferation of TF-1 cells was found to be < 0.5ng/ml, corresponding to a specific activity of > 2.0×106 units/mg.
What is the amino acid sequence of CTF1 Protein?
MSQREGSLED HQTDSSFSFL PHLEAKIRQT HNLARLLTKY ADQLLEEYVQ QQGEPFGLPG FSPPRLPLAG LSGPAPSHAG LPVSERLRQD AAALSALPAL LDAVRRRQAE LNPRAPRLLR SLEDAARQVR ALGAAVETVL AALGAAARGP VPEPVATSAL FTSNSAAGVF SAKVLGLHVC GLYGEWVSRT EGDLGQLVPG GVA.
What applications can CTF1 Protein be used in?
CTF1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CTF1 Protein?
The endotoxin level is minimal, CTF1 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 :
NANOG Human, HisDescription:
Nanog Human Recombinant, His Tag
NANOG, Homeobox protein NANOG, Homeobox transcription factor Nanog, hNanog.
Product # :
PRO-881Price :
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Shipped with Ice Packs
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Description
NANOG Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 174 amino acids (1-154) and having a molecular mass of 19.6 kDa.The NANOG is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NANOG protein (0.25mg/ml) is supplied in 20mM Tris-HCL, pH-8, 1mM DTT and 20% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
NANOG is a multidomain homeobox transcription factor which functions to maintain the undifferentiated state of pluripotent stem cells. NANOG expression counteracts the differentiation-promoting signals induced by the extrinsic factors LIF, Stat3 and BMP. Once NANOG expression is downregulated, cell differentiation can proceed. Proteins which regulate NANOG expression include transcription factors Oct4, SOX2, FoxD3, and Tcf3 and tumor suppressor p53.
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Synonyms
NANOG, Homeobox protein NANOG, Homeobox transcription factor Nanog, hNanog.
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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 MSVDPACPQS LPCFEASDCK ESSPMPVICG PEENYPSLQM SSAEMPHTET VSPLPSSMDL LIQDSPDSST SPKGKQPTSA EKSVAKKEDK VPVKKQKTRT VFSSTQLCVL NDRFQRQKYL SLQQMQELSN ILNLSYKQVK TWFQNQRMKS KRWQ
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 :
NRGN HumanDescription:
Neurogranin Human Recombinant
hng, RC3, Neurogranin, Ng, NRGN.
Product # :
CYT-293Price :
Quantity :
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Shipped with Ice Packs
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Description
NRGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (1-78 a.a.) and having a molecular mass of 10.0kDa (molecular size on SDS-PAGE will appear higher). NRGN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NRGN protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH7.0), 30% glycerol 0.1mM PMSF and 1mM EDTA.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Neurogranin (NRGN) is a calmodulin-binding protein which is expressed solely in the brain, mainly in dendritic spines. NRGN is also taking part in the protein kinase C signaling pathway by being a "third messenger" substrate of protein kinase C-mediated molecular cascades during synaptic development and remodeling. NRGN binds to calmodulin in the absence of calcium. NRGN protein’s phosphorylation by protein kinase C lowers its binding ability.
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Synonyms
hng, RC3, Neurogranin, Ng, NRGN.
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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 MGSMDCCTEN ACSKPDDDIL DIPLDDPGAN AAAAKIQASF RGHMARKKIK SGERGRKGPG PGGPGGAGVA RGGAGGGPSG D.
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 :
STOML1 HumanDescription:
Stomatin Like 1 Human Recombinant
Stomatin (EPB72)-Like 1, STORP, Stomatin-Related Protein, Stomatin (EBP72)-Like 1, Protein Unc-24 Homolog, EPB72-Like Protein 1, SLP-1, Stomatin-Like Protein 1, Stomatin-Like 1, HUNC-24, UNC24, SLP1.
Product # :
PRO-2164Price :
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Shipped with Ice Packs
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Description
STOML1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (79-398 a.a) and having a molecular mass of 37kDa.STOML1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
STOML1 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Stomatin Like 1, also known as STOML1, is a protein coding gene which is a part of the band 7/mec-2 family. STOML1 contains one SCP2 domain and expressed at low levels. STOML1 acts as an ion channel inhibitor.
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Synonyms
Stomatin (EPB72)-Like 1, STORP, Stomatin-Related Protein, Stomatin (EBP72)-Like 1, Protein Unc-24 Homolog, EPB72-Like Protein 1, SLP-1, Stomatin-Like Protein 1, Stomatin-Like 1, HUNC-24, UNC24, SLP1.
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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).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSLKIVPTY ERMIVFRLGR IRTPQGPGMV LLLPFIDSFQ RVDLRTRAFN VPPCKLASKD GAVLSVGADV QFRIWDPVLS VMTVKDLNTA TRMTAQNAMT KALLKRPLRE IQMEKLKISD QLLLEINDVT RAWGLEVDRV ELAVEAVLQP PQDSPAGPNL DSTLQQLALH FLGGSMNSMA GGAPSPGPAD TVEMVSEVEP PAPQVGARSS PKQPLAEGLL TALQPFLSEA LVSQVGACYQ FNVVLPSGTQ SAYFLDLTTG RGRVGHGVPD GIPDVVVEMA EADLRALLCR ELRPLGAYMS GRLKVKGDLA MAMKLEAVLR ALK.
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 :
FABP4 Human, HisDescription:
Fatty Acid Binding Protein 4 Human Recombinant, His Tag
Fatty acid-binding protein adipocyte, AFABP, Fatty acid-binding protein 4, Adipocyte lipid-binding protein, ALBP, A-FABP, FABP4.
Product # :
PRO-566Price :
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Shipped with Ice Packs
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Description
FABP4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids and having a molecular mass of 18 kDa. FABP4 is fused to His tag at N-terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
FABP4 His-Tag is supplied in 20mM Tris HCL pH=8, 0.5mM DTT and 50% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Adipocyte fatty acid binding protein FABP4 is a 15 kDa member of the intracellular fatty acid binding protein (FABP) family, which is known for the ability to bind fatty acids and related compounds (bile acids or retinoids) in an internal cavity. FABP4 is expressed in a differentiation-dependent fashion in adipocytes and is a critical gene in the regulation of the biological function of these cells.
In mice, targeted mutations in FABP4 provide significant protection from hyperinsulinemia and insulin resistance in the context of both dietary and genetic obesity. Adipocytes obtained from FABP4-deficient mice also have reduced efficiency of ipolysis in vitro and in vivo, and these mice exhibited moderately improved systemic dyslipidemia. Recent studies also demonstrated FABP4 expression in macrophages upon differentiation and activation. In these cells, FABP4 modulates inflammatory responses and cholesterol ester accumulation, and total or macrophage-specific FABP4 deficiency confers dramatic protection against atherosclerosis in the apoE-/- mice. These results indicate a central role for FABP4 in the development of major components of the metabolic syndrome through its distinct actions in adipocytes and macrophages. -
Synonyms
Fatty acid-binding protein adipocyte, AFABP, Fatty acid-binding protein 4, Adipocyte lipid-binding protein, ALBP, A-FABP, FABP4.
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Physical Appearance
Sterile Filtered colorless liquid formulation.
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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.Please avoid freeze thaw cycles.
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 :
THBD HumanDescription:
Thrombomodulin Human Recombinant
THBD, Thrombomodulin, TM, Fetomodulin, CD141, CD141 antigen, THRM, BDCA-3, BDCA3, blood dendritic cell antigen 3, AHUS6, THPH12.
Product # :
PRO-2697Price :
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Shipped with Ice Packs
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Description
THBD Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 500 amino acids (22-515a.a) and having a molecular mass of 52.6kDa.THBD is fused to an 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
THBD protein solution (0.5mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Thrombomodulin, also referred to THBD, is an endothelial cell-expressed, transmembrane glycoprotein that can form a complex with the coagulation factor, thrombin. This complex increasethe activation of protein C in the anticoagulant pathway by forming a 1:1 stoichiometric complex with thrombin. Thrombomodulinbound thrombin has procoagulant effect at the same time by inhibiting fibrinolysis by cleaving thrombinactivatable fibrinolysis inhibitor (TAFI) into its active form. Reduced levels of thrombomodulin or increased serum levels of THBD can correlate with pathogenesis of certain cardiovascular diseases, such as atherosclerosis and thrombosis. Furthermore, it associated with, diabetes mellitus, liver cirrhosis, cerebral & myocardial infarction, and multiple sclerosis.
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Synonyms
THBD, Thrombomodulin, TM, Fetomodulin, CD141, CD141 antigen, THRM, BDCA-3, BDCA3, blood dendritic cell antigen 3, AHUS6, THPH12.
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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
EPQPGGSQCV EHDCFALYPG PATFLNASQI CDGLRGHLMT VRSSVAADVI SLLLNGDGGV GRRRLWIGLQ LPPGCGDPKR LGPLRGFQWV TGDNNTSYSR WARLDLNGAP LCGPLCVAVS AAEATVPSEP IWEEQQCEVK ADGFLCEFHF PATCRPLAVE PGAAAAAVSI TYGTPFAARG ADFQALPVGS SAAVAPLGLQ LMCTAPPGAV QGHWAREAPG AWDCSVENGG CEHACNAIPG
APRCQCPAGA ALQADGRSCT ASATQSCNDL CEHFCVPNPD QPGSYSCMCE TGYRLAADQH RCEDVDDCIL EPSPCPQRCV NTQGGFECHC YPNYDLVDGE CVEPVDPCFR ANCEYQCQPL NQTSYLCVCA EGFAPIPHEP HRCQMFCNQT ACPADCDPNT QASCECPEGY ILDDGFICTD IDECENGGFC SGVCHNLPGT FECICGPDSA LARHIGTDCD SGKVDGGDSG SGEPPPSPTP
GSTLTPPAVG LVHSHHHHHH
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 :
TIMP1 Human, HEKDescription:
Tissue Inhibitor of Metalloprotease 1 Human Recombinant, HEK
Metalloproteinase inhibitor 1, Tissue inhibitor of metalloproteinases, TIMP-1, Erythroid-potentiating activity, EPA, TIMP1, CLGI, TIMP, EPO, HCI, FLJ90373.
Product # :
ENZ-508Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TIMP1 Human Recombinant produced in HEK-293 cells is a secreted protein with the sequence of Human TIMP-1 (amino acids Cys24-Ala207) and fused to a polyhistidine tag at the C-terminus.
Source
HEK293 Cells.
Formulation
The TIMP1 protein was lyophilized after extensive dialysis against PBS.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The IC50 of 2.5-4 nM is measured by its ability to inhibit recombinant human MMP-2 cleavage of the colorimetric peptide substrate, Mca-PLGL-DpaAR-NH2.Citations
More Info
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Introduction
TIMP1 is a member of the TIMP family. TIMP1 is an inducible glycoprotein produced by various cell types. The TIMP1 glycoprotein is a natural inhibitor of the matrix metalloproteinases, which a group of peptidases involved in degradation of the extracellular matrix. TIMP1 binds in a reversible mode to MMPs, with regions in the N-terminal domain binding to the MMP substrate-binding site. On top of its inhibitory function against most of the known MMPs, TIMP1 is able to promote cell proliferation in a broad range of cell types, and may also have an anti-apoptotic role. Furthermore, TIMP1 has erthyroid-potentiating activity via translocation to the nucleus and also inhibits apoptosis in B-cells. The TIMP1 gene is situated within intron 6 of the synapsin I gene and is transcribed in the opposite direction. TIMP1 activity is dependent on the existence of disulfide bonds. TIMP1 transcription is extremely inducible in reaction to many cytokines and hormones. Increased TIMP1 levels are connecte
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Synonyms
Metalloproteinase inhibitor 1, Tissue inhibitor of metalloproteinases, TIMP-1, Erythroid-potentiating activity, EPA, TIMP1, CLGI, TIMP, EPO, HCI, FLJ90373.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TIMP1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TIMP1 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 TIMP1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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 :
G CSF Human, HisDescription:
Granulocyte-Colony Stimulating Factor Human Recombinant, His Tag
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
Product # :
CYT-476Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- formulation
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Description
Granulocyte Colony Stimulating Factor-His Tag Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 174 amino acids, fragment (31-204) and having a molecular mass of 23.19 kDa with an amino-terminal hexahistidine tag.G-CSF-His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Granulocyte Colony Stimulating Factor His is supplied in 1x PBS and 50% glycerol.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
Granulocyte Colony Stimulating Factor is a growth factor and/or cytokine produced by the endothelium, macrophages and a number of other immune cells. GCSF stimulates the bone marrow to produce granulocytes and also to stimulate the survival, proliferation, differentiation and function of neutrophil granulocyte progenator cells and mature neutrophils.
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Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
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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. Please avoid freeze thaw cycles.
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Background
What is the molecular weight/Mw of G CSF Protein?
G CSF Protein has a total Mw of 23.19kDa.
What is the source or expression system of G CSF Protein?
Escherichia Coli.
What is the Purity of G CSF Protein?
G CSF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of G CSF Protein?
The biological functionality of G CSF Protein will be determined in the future.
What is the amino acid sequence of G CSF Protein?
G CSF Protein is composed from 174 amino acids.
What applications can G CSF Protein be used in?
G CSF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for G CSF Protein?
The endotoxin level is minimal, G CSF 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 :
Glucagon ReceptorDescription:
Glucagon Receptor Human Recombinant
GL-R, GLR, Glucagon Receptor.
Product # :
HOR-020Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
GCGR Human Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain (a.a 29-142) containing 125 amino acids including an 8 a.a C-terminal His tag. The total molecular mass is 19.9kDa (calculated).
Source
E. coli
Formulation
GCGR filtered (0.4 µm) and lyophilized from solution in acetonitrile/0,1%TFA and 1% (w/v) trehalose.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Glucagon receptor is part of the glucagon receptor family which also contains GLP-1, GLP-2, GHRH and GIP receptors. GCGR regulates blood glucose levels and is mainly expressed in the pancreas, liver and kidneys. Mutations in GCGR are a cause of non-insulin-dependent diabetes mellitus.
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Synonyms
GL-R, GLR, Glucagon Receptor.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after one week at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. GCGR is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MQVMDFLFEK WKLYGDQCHH NLSLLPPPTE LVCNRTFDKY SCWPDTPANT TANISCPWYL PWHHKVQHRF VFKRCGPDGQ WVRGPRGQPW RDASQCQMDG EEIEVQKEVA KMYSSFQLEH HHHHH.
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Background
What is the molecular weight/Mw of GLUCAGON RECEPTOR Protein?
GLUCAGON RECEPTOR Protein has a total Mw of 19.9kDa.
What is the source or expression system of GLUCAGON RECEPTOR Protein?
Escherichia Coli.
What is the Purity of GLUCAGON RECEPTOR Protein?
GLUCAGON RECEPTOR Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of GLUCAGON RECEPTOR Protein?
The biological functionality of GLUCAGON RECEPTOR Protein will be determined in the future.
What is the amino acid sequence of GLUCAGON RECEPTOR Protein?
MQVMDFLFEK WKLYGDQCHH NLSLLPPPTE LVCNRTFDKY SCWPDTPANT TANISCPWYL PWHHKVQHRF VFKRCGPDGQ WVRGPRGQPW RDASQCQMDG EEIEVQKEVA KMYSSFQLEH HHHHH.
What applications can GLUCAGON RECEPTOR Protein be used in?
GLUCAGON RECEPTOR Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GLUCAGON RECEPTOR Protein?
The endotoxin level is minimal, GLUCAGON RECEPTOR Protein was purified using conventional chromatography techniques.
Who supplies recombinant GLUCAGON RECEPTOR that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of GLUCAGON RECEPTOR?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
PPIL4 HumanDescription:
Peptidylprolyl Isomerase (Cyclophilin)-Like 4 Human Recombinant
Peptidyl-prolyl cis-trans isomerase-like 4, PPIase, Cyclophilin-like protein PPIL4, Rotamase PPIL4, PPIL4, HDCME13P.
Product # :
ENZ-026Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PPIL4 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 512 amino acids (1-492 a.a.) and having a molecular mass of 59.3kDa. The PPIL4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PPIL solution (0.5 mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 190 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.Citations
More Info
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Introduction
PPIL4 belongs to an evolutionarily conserved cyclophilin-type PPIase family of proteins. PPIL4, which is ubiquitously expressed with predominant expression in kidney localizes to the nucleus and contains one PPIase cyclophilin-type domain, a lysine-rich domain, a pair of bipartite nuclear targeting sequences and one RRM (RNA recognition motif) domain. The presence of the RRM domain along with nuclear targeting sequences implies that PPIL4 may be involved in transcriptional regulation.
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Synonyms
Peptidyl-prolyl cis-trans isomerase-like 4, PPIase, Cyclophilin-like protein PPIL4, Rotamase PPIL4, PPIL4, HDCME13P.
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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 MAVLLETTLG DVVIDLYTEE RPRACLNFLK LCKIKYYNYC LIHNVQRDFI IQTGDPTGTG RGGESIFGQL YGDQASFFEA EKVPRIKHKK KGTVSMVNNG SDQHGSQFLI TTGENLDYLD GVHTVFGEVT EGMDIIKKIN ETFVDKDFVP YQDIRINHTV ILDDPFDDPP DLLIPDRSPE PTREQLDSGR IGADEEIDDF KGRSAEEVEE IKAEKEAKTQ AILLEMVGDL PDADIKPPEN VLFVCKLNPV TTDEDLEIIF SRFGPIRSCE VIRDWKTGES LCYAFIEFEK EEDCEKAFFK MDNVLIDDRR IHVDFSQSVA KVKWKGKGGK YTKSDFKEYE KEQDKPPNLV LKDKVKPKQD TKYDLILDEQ AEDSKSSHSH TSKKHKKKTH HCSEEKEDED YMPIKNTNQD IYREMGFGHY EEEESCWEKQ KSEKRDRTQN RSRSRSRERD GHYSNSHKSK YQTDLYERER SKKRDRSRSP KKSKDKEKSK YR.
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 :
TSPAN7 HumanDescription:
Tetraspanin 7 Human Recombinant
Tspan-7, Cell surface glycoprotein A15, Membrane component chromosome X surface marker 1, T-cell acute lymphoblastic leukemia-associated antigen 1, TALLA-1, Transmembrane 4 superfamily member 2, CD231, A15, DXS1692E, MXS1, TM4SF2.
Product # :
PRO-2414Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TSPAN7 Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 110 amino acids (113-213a.a.) and having a molecular mass of 12.6kDa. (Molecular size on SDS-PAGE under reducing conditions 13.5-18kDa). TSPAN7 is expressed with a 6amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
TSPAN7 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Tetraspanin 7, also known as TSPAN7, is part of the transmembrane 4 superfamily, which is also familiar as the tetraspanin family. Most of these proteins mediate signal transduction events which play a role in the regulation of cell development, activation, growth as well as motility. Furthermore, TSPAN7 is associated with X-linked mental retardation in addition to neuropsychiatric diseases such as Huntington's chorea, fragile X syndrome and myotonic dystrophy. Lately, TSPAN7 has been acknowledged as a key immune system target in type 1 diabetes.
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Synonyms
Tspan-7, Cell surface glycoprotein A15, Membrane component chromosome X surface marker 1, T-cell acute lymphoblastic leukemia-associated antigen 1, TALLA-1, Transmembrane 4 superfamily member 2, CD231, A15, DXS1692E, MXS1, TM4SF2.
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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
ADPRHEIKDT FLRTYTDAMQ TYNGNDERSR AVDHVQRSLS CCGVQNYTNW STSPYFLEHG IPPSCCMNET DCNPQDLHNL TVAATKVNQK GCYDLVTSFM ETNMHHHHHH.
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 :
LGALSL HumanDescription:
Lectin Galactoside-Binding-Like Human Recombinant
GRP, HSPC159, Galectin-related protein, Lectin galactoside-binding-like protein, LGALSL.
Product # :
PRO-1374Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LGALSL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 195 amino acids (1-172a.a) and having a molecular mass of 21.4kDa. LGALSL is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
LGALSL protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Galectins are a family of soluble b-galactoside-binding animal lectins that modulate cell-to-cell adhesion and cell-to-extracellular matrix interactions. Galectins also take part in tumor progression, pre-mRNA splicing and apoptosis. Galectin-related protein (LGALSL) is a 172 amino acid protein which holds one galectin domain. In spite of this, LGALSL does not appear to bind carbohydrates or lactose since the critical residues required for binding are not conserved.
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Synonyms
GRP, HSPC159, Galectin-related protein, Lectin galactoside-binding-like protein, LGALSL.
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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 MGSMAGSVAD SDAVVKLDDG HLNNSLSSPV QADVYFPRLI VPFCGHIKGG MRPGKKVLVM GIVDLNPESF AISLTCGDSE DPPADVAIEL KAVFTDRQLL RNSCISGERG EEQSAIPYFP FIPDQPFRVE ILCEHPRFRV FVDGHQLFDF YHRIQTLSAI DTIKINGDLQ ITKLG.
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 :
MAGEA3 HumanDescription:
Melanoma Antigen Family A, 3 Human Recombinant
CT1.3, MAGE3, HYPD, Melanoma Antigen family A, 3, MAGE-3 antigen, MAGEA6, Antigen MZ2-D, Melanoma-Associated antigen 3.
Product # :
PRO-502Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MAGEA3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 337 amino acids (1-314 a.a.) and having a molecular mass of 37.1kDa.MAGEA3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MAGEA3 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) 1mM DTT, 100mM NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
MAGE belongs to the MAGE gene family, that comprises 12 known genes, of which 6 are expressed in tumors. The Melanoma-associated antigen 3 genes were originally isolated from different kinds of tumors, and based on their virtually limited tumor-specific expression in adult tissues, they were used as targets for cancer immunotherapy. MAGEA3 is a tumor-specific antigen extensively expressed in solid and hematologic malignancies, but not in normal tissues, with the exclusion of testis and placenta. Consequently, MAGEA3 is an outstanding candidate tumor antigen.
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Synonyms
CT1.3, MAGE3, HYPD, Melanoma Antigen family A, 3, MAGE-3 antigen, MAGEA6, Antigen MZ2-D, Melanoma-Associated antigen 3.
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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 MGSMPLEQRS QHCKPEEGLE ARGEALGLVG AQAPATEEQE AASSSSTLVE VTLGEVPAAE SPDPPQSPQG ASSLPTTMNY PLWSQSYEDS SNQEEEGPST FPDLESEFQA ALSRKVAELV HFLLLKYRAR EPVTKAEMLG SVVGNWQYFF PVIFSKASSS LQLVFGIELM EVDPIGHLYI FATCLGLSYD GLLGDNQIMP KAGLLIIVLA IIAREGDCAP EEKIWEELSV LEVFEGREDS ILGDPKKLLT QHFVQENYLE YRQVPGSDPA CYEFLWGPRA LVETSYVKVL HHMVKISGGP HISYPPLHEW VLREGEE
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 :
CKMB HumanDescription:
Creatine Kinase MB Human Recombinant
CKMB, CK-MB
Product # :
CKI-286Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human Creatine Kinase MB produced in E.Coli is a single, non-glycosylated, polypeptide chain, having a molecular weight of ~44kDa.The CKMB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein solution contains 50mM Tris-HCL, 5mM B-mercaptoethanol, 1mM EDTA, 5mM disodium Succinate, Ph 8.0 and 50% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
The three isoenzymes (MM, MB, and BB) are found in muscle, cardiac and brain tissues. These recombinant proteins are ideal for calibrating diagnostic instruments and researching neuromuscular diseases. Creatine Kinases can be used for indications in many neuromuscular applications. These disorders include cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle's disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, rheumatic diseases, and other that create elevated or reduced levels of Creatine Kinases.
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Physical Appearance
Sterile Filtered colorless liquid formulation.
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Stability
CKMB although stable at 10°C for 7 days, should be stored below -18°C.Please prevent freeze-thaw cycles.
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 :
AREG HumanDescription:
Amphiregulin Human Recombinant
Schwannoma-derived growth factor, Colorectum cell-derived growth factor, AR, CRDGF, SDGF, AREGB, MGC13647.
Product # :
CYT-041Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Amphiregulin (AREG) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 98 amino acids and having a molecular mass of 11.3 KDa.The AREG is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to stimulate the proliferation of mouse Balb/c 3T3 cells. The expected ED50 for this effect is 5-10 ng/ml, corresponding to a specific activity of 100,000-200,000units/mg.Citations
More Info
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Synonyms
Schwannoma-derived growth factor, Colorectum cell-derived growth factor, AR, CRDGF, SDGF, AREGB, MGC13647.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized AREG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution AREG 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 AREG 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
SVRVEQVVKP PQNKTESENT SDKPKRKKKG GKNGKNRRNR KKKNPCNAEF QNFCIHGECK YIEHLEAVTC KCQQEYFGER CGEKSMKTHS MIDSSLSK.
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Background
Amphiregulin Human Recombinant: Exploring its Role in Cancer Biology and Therapeutic Applications
Abstract:
Amphiregulin, a member of the epidermal growth factor (EGF) family, has gained significant attention in cancer research. This research paper provides an overview of Amphiregulin human recombinant, highlighting its molecular characteristics, signaling pathways, and therapeutic potential. Understanding the multifaceted role of Amphiregulin opens avenues for targeted cancer therapies. This article provides a concise analysis of Amphiregulin, emphasizing its impact on cancer biology and its therapeutic applications.Introduction:
Cancer continues to be a significant health challenge worldwide, necessitating novel therapeutic approaches. Amphiregulin, an EGF family member, has emerged as a promising target in cancer research. This paper provides an overview of Amphiregulin, shedding light on its structure, function, and therapeutic potential.Amphiregulin Signaling and Mechanisms:
Amphiregulin exerts its effects through the binding and activation of the EGF receptor (EGFR). Upon activation, a cascade of intracellular signaling pathways is triggered, including the MAPK and PI3K/AKT pathways. These pathways regulate critical cellular processes such as cell proliferation, survival, migration, and angiogenesis.Amphiregulin in Cancer Biology:
Amphiregulin has been implicated in various aspects of cancer biology, including tumor growth, metastasis, and resistance to therapy. Its overexpression is observed in several cancer types, and its role in promoting tumor growth and metastasis has been demonstrated in preclinical studies. Targeting Amphiregulin signaling shows promise in inhibiting cancer progression and overcoming therapy resistance.Therapeutic Potential of Amphiregulin Human Recombinant:
Amphiregulin human recombinant holds significant therapeutic potential in cancer treatment. Strategies aimed at blocking Amphiregulin-EGFR interactions or inhibiting downstream signaling pathways are being explored as potential therapeutic interventions. Additionally, Amphiregulin could serve as a predictive biomarker to identify patients who are more likely to respond to targeted therapies.Challenges and Future Directions:
While the therapeutic targeting of Amphiregulin shows promise, several challenges need to be addressed. Further research is required to fully understand the complex interplay between Amphiregulin and other molecular pathways in cancer biology. Additionally, the development of specific and potent inhibitors and the identification of patient selection criteria are important considerations for successful clinical translation.Conclusion:
Amphiregulin human recombinant represents a promising avenue for targeted cancer therapy. Understanding the molecular mechanisms and functional implications of Amphiregulin in cancer biology offers new opportunities for developing innovative treatments. Continued research in this field has the potential to improve patient outcomes and contribute to the advancement of personalized medicine.What is the molecular weight/Mw of AREG Protein?
AREG Protein has a total Mw of 11.3kDa.
What is the source or expression system of AREG Protein?
Escherichia Coli.
What is the Purity of AREG Protein?
AREG Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of AREG Protein?
Determined by its ability to stimulate the proliferation of mouse Balb/c 3T3 cells. The expected ED50 for this effect is 5-10 ng/ml, corresponding to a specific activity of 100,000-200,000units/mg.
What is the amino acid sequence of AREG Protein?
SVRVEQVVKP PQNKTESENT SDKPKRKKKG GKNGKNRRNR KKKNPCNAEF QNFCIHGECK YIEHLEAVTC KCQQEYFGER CGEKSMKTHS MIDSSLSK.
What applications can AREG Protein be used in?
AREG Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for AREG Protein?
The endotoxin level is minimal, AREG 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 :
Histone BovineDescription:
Bovine Histone
Product # :
PRO-2558Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Histone Bovine is purified from bovine tissues by proprietary protein-chemical techniques.
Source
Bovine tissues.
Formulation
Histone Bovine is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Histone is vastly alkaline protein exists in eukaryotic cell nuclei which set and direct the DNA into structural units named nucleosomes. 5 key families of histones are: H1/H5, H2A, H2B, H3, including H4. The core histones are H2A, H2B, H3 and H4, whereas histones H1/H5 are identified as the linker histones. Moreover the dynamics of chromatin structure depend on posttranslational modification of histones in addition to the appearance of different histone variants. Histone H3 as well as H4 are modified covalently at several residues. The histone code is constitute by these and the H2A/H2B modifications.
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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. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG type human auto antibodies.2. Checkerboard/immunodot analysis of positive/negative samples.
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coating concentration
0.2-0.5 μg/ml (depending on the type of ELISA plate and coating buffer). Suitable for labeling of functional groups.
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 :
CRYGN HumanDescription:
Crystallin, Gamma N Human Recombinant
Gamma-crystallin N, Gamma-N-crystallin, CRYGN.
Product # :
PRO-1152Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CRYGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (1-182 a.a) and having a molecular mass of 23.1kDa.CRYGN is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CRYGN protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Crystallin gamma N (CRYGN) is a member of the Crystallins family. Crystallins are the main proteins of the vertebrate eye lens, where they preserve the transparency and refractive index of the lens. CRYGN is unique in the way that it has both beta and gamma crystallin protein motifs. The CRYGN is differentially controlled after early development, and is involved in cataract creation due to either age-related protein degradation or genetic mutation.
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Synonyms
Gamma-crystallin N, Gamma-N-crystallin, CRYGN.
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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 MGSHMAQRSG KITLYEGKHF TGQKLEVFGD CDNFQDRGFM NRVNSIHVES GAWVCFNHPD FRGQQFILEH GDYPDFFRWN SHSDHMGSCR PVGMHGEHFR LEIFEGCNFT GQCLEFLEDS PFLQSRGWVK NCVNTIKVYG DGAAWSPRSF GAEDFQLSSS LQSDQGPEEA TTKPATTQPP FLTANL.
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 :
HES7 HumanDescription:
Hairy and Enhancer of Split 7 Human Recombinant
Hairy and enhancer of split 7, bHLHb37, SCDO4, Transcription factor HES-7, HES7, hHes7, Class B basic helix-loop-helix protein 37, bHLH factor Hes7.
Product # :
PRO-1306Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HES7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 253 amino acids (1-230) and having a molecular mass of 27kDa. HES7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HES7 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
HES7 belongs to the Hairy and enhancer of split family of bHLH transcription factors. The mouse ortholog of the HES7 is set by Notch signaling. The protein serves as a transcriptional repressor, and is involved in correct patterning of the axial skeleton. A mutation in HES7 has been shown to result in spondylocostal dysostosis. Multiple transcript variants encoding different isoforms have been discovered for HES7.
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Synonyms
Hairy and enhancer of split 7, bHLHb37, SCDO4, Transcription factor HES-7, HES7, hHes7, Class B basic helix-loop-helix protein 37, bHLH factor Hes7.
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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 MGSMVTRDRA ENRDGPKMLK PLVEKRRRDR INRSLEELRL LLLERTRDQN LRNPKLEKAE ILEFAVGYLR ERSRVEPPAA AAPGVPRSPV QDAEALASCY LSGFRECLLR LAAFAHDASP AARAQLFSAL HGYLRPKPPR PKPVDPRPPA PRPSLDPAAP ALGPALHQRP PVHQGHPSPR CAWSPSLCSP RAGDSGAPAP LTGLLPPPPP PHRQDGAPKA PLPPPPAFWR PWP.
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 :
CUTC HumanDescription:
cutC Copper Transporter Homolog Human Recombinant
Copper homeostasis protein cutC homolog, CUTC, CGI-32, RP11-483F11.3.
Product # :
PRO-911Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
CUTC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 293 amino acids (1-273 a.a) and having a molecular mass of 31.5kDa.CUTC is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CUTC protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 10% glycerol and 200mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CUTC belongs to the Cut family and may be involved in efflux trafficking of cuprous ion. The Cut family is linked with the copper homeostasis and involved in several vital metabolisms, such as uptake, storage, delivery, and efflux of copper. Copper which is an essential heavy metal trace element has an imperative role in cell physiology.
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Synonyms
Copper homeostasis protein cutC homolog, CUTC, CGI-32, RP11-483F11.3.
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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 MKRQGASSER KRARIPSGKA GAANGFLMEV CVDSVESAVN AERGGADRIE LCSGLSEGGT TPSMGVLQVV KQSVQIPVFV MIRPRGGDFL YSDREIEVMK ADIRLAKLYG ADGLVFGALT EDGHIDKELC MSLMAICRPL PVTFHRAFDM VHDPMAALET LLTLGFERVL TSGCDSSALE GLPLIKRLIE QAKGRIVVMP GGGITDRNLQ RILEGSGATE FHCSARSTRD SGMKFRNSSV AMGASLSCSE YSLKVTDVTK VRTLNAIAKN ILV.
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 :
DCTN6 HumanDescription:
Dynactin 6 Human Recombinant
Dynactin 6, WS3, Dynactin Subunit P27, Protein WS-3, P27, Novel RGD-Containing Protein, Dynactin Subunit 6, WS-3, Dynactin subunit 6.
Product # :
PRO-2094Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DCTN6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213 amino acids (1-190 a.a) and having a molecular mass of 23.1kDa. DCTN6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DCTN6 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Dynactin 6, also known as DCTN6 is a member of the dynactin subunits 5/6 family. DCTN6 includes an RGD (Arg-Gly-Asp) motif in the N-terminal region, which confers adhesive properties to macromolecular proteins such as fibronectin. DCTN6 has a high degree of sequence resemblance with the mouse homolog, which has been found to participate in mitochondrial biogenesis. Moreover, the precise biological function of DCTN6 is unknown.
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Synonyms
Dynactin 6, WS3, Dynactin Subunit P27, Protein WS-3, P27, Novel RGD-Containing Protein, Dynactin Subunit 6, WS-3, Dynactin subunit 6.
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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 MGSMAEKTQK SVKIAPGAVV CVESEIRGDV TIGPRTVIHP KARIIAEAGP IVIGEGNLIE EQALIINAYP DNITPDTEDP EPKPMIIGTN NVFEVGCYSQ AMKMGDNNVI ESKAYVGRNV ILTSGCIIGA CCNLNTFEVI PENTVIYGAD CLRRVQTERP QPQTLQLDFL MKILPNYHHL KKTMKGSSTP VKN.
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 :
ARPP19 HumanDescription:
CAMP-Regulated Phosphoprotein, 19kDa Human Recombinant
CAMP-Regulated Phosphoprotein 19kDa, ARPP-19, ARPP16, Endosulfine Alpha-Like, ARPP-16, ENSAL, CAMP-Regulated Phosphoprotein 19, Cyclic AMP Phosphoprotein 19 KD, ARPP19.
Product # :
PRO-1785Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ARPP19 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 135 amino acids (1-112 a.a) and having a molecular mass of 14.7kDa.ARPP19 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ARPP19 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
cAMP-regulated phosphoprotein 19 (ARPP19) is protein phosphatase inhibitor which specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-62 during mitosis, ARPP19 specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, a vital condition to maintain cyclin-B1-CDK1 activity high during M phase. ARPP19 protein may indirectly boost GAP-43 expression. The 19 kDa cAMP-regulated phosphoprotein has a role in regulating mitosis by obstructing protein phosphatase-2A.
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Synonyms
CAMP-Regulated Phosphoprotein 19kDa, ARPP-19, ARPP16, Endosulfine Alpha-Like, ARPP-16, ENSAL, CAMP-Regulated Phosphoprotein 19, Cyclic AMP Phosphoprotein 19 KD, ARPP19.
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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 MGSMSAEVPE AASAEEQKEM EDKVTSPEKA EEAKLKARYP HLGQKPGGSD FLRKRLQKGQ KYFDSGDYNM AKAKMKNKQL PTAAPDKTEV TGDHIPTPQD LPQRKPSLVA SKLAG.
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.