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1000 results found for “Crystallin”
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Name :
ChitodextrinaseDescription:
Chitodextrinase Clostridium Botulinum Recombinant
Product # :
ENZ-032Price :
Quantity :
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Shipped at Room temp
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Description
Chitodextrinase Clostridium Botulinum Recombinant fused with a 13 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 590 amino acids and having a molecular mass of 66.9kDa. The Chitodextrinase is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Chitodextrinase lyophilized from a 0.2µm filtered concentrated solution in PBS.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Chitodextrinase is a unique membrane-bound endoenzyme. The chitodextrinase enzyme cleaves soluble oligomers, but not chitin, to the di- and trisaccharides. Chitodextrinase is unable to solubilize chitin, but it can catalyze the hydrolysis of high to low molecular weight soluble chitin oligosaccharides.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Chitodextrinase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Chitodextrinase 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 Chitodextrinase in sterile 18MΩ-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
HMRGSGSHHHHHHKEKFKTTKIKNSSELNRKLVGYFPEWAYSSEAQGYFNVTD
LQWDSLTHIQYSFAMVDPSTNKITLSNKHAAIEEDFSEFDLNYNGKKIELDPS
LPYKGHFNVLQTMKKNYPDVSLLISVGGWTGTRCFYTMIDTDNRINTFADSCV
DFIRKYGFDGVDIDFEYPSSTSQSGNPDDFDLSEPRRTKLNERYNILIKTLRE
KIDMASKEDGKEYLLTAAVTASPWVLGGISDNTYAKYLDFLSIMSYDYHGGWN
EYVEHLAGIYPNKEDRETVTQIMPTLCMDWAYRYYRGVLPAEKILMGIPYYTR
GWENVQGGINGLHGSSKTPASGKYNILGDDLNNDGVLEPDGANPLWHVLNLME
QDPNLKVYWDEISKVPYVWQNDKKVFVSFENEKSIDARLEYIQNKNLGGALIW
VMNGDYGLNPNYVEGSNKINEGKYTFGDTLTKRLSQGLKKMGVCNKTPDDLNI
SLEPINVDVKFNGKYDHPNYTYSIDITNYTDKEIKGGWNVSFDLPKSAVFKSS
WGGTYSVTDNGDFNTITLTSGAWQNIAPNSTITVQGMIGLCFSGIRNVTFNGM
NPIGNDK.
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 :
S100A11 HumanDescription:
S100 Calcium Binding Protein A11 Human Recombinant
Protein S100-A11, S100 calcium-binding protein A11, Calgizzarin, MLN 70, S100A11, MLN70, S100C.
Product # :
PRO-385Price :
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Description
S100A11 Human Recombinant is expressed in E. coli having a molecular weight of 17kDa fused to an amino terminal hexahistidine tag.
Source
Escherichia Coli.
Formulation
S100A11 is supplied in PBS and 50% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
2 bands on Western blot at 17 and 34 kDa, respectively representing monomeric and dimeric form.Citations
More Info
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Introduction
S100A11 is a member of the S100 family of proteins which contains two EF-hand calcium-binding motifs and is thought to be involved in the regulation of a number of cellular processes including cell cycle progression and differentiation. S100A11 may function in motility, invasion and tubulin polymerisation. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21. Chromosomal rearrangements and altered expression of S100A11 have been implicated in tumor metastasis.
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Synonyms
Protein S100-A11, S100 calcium-binding protein A11, Calgizzarin, MLN 70, S100A11, MLN70, S100C.
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Stability
Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Applications
S100A11 can be used directly as a positive control in Western blotting, ELISA, immunoprecipitation and other immunological experiments.
The biological activity of this product has not yet been tested.
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 :
CDH2 HumanDescription:
Cadherin 2 Human Recombinant
Cadherin 2, Cadherin 2, Type 1, N-Cadherin (Neuronal), Neural Cadherin, N-Cadherin, CDw325, NCAD, CDHN, Calcium-Dependent Adhesion Protein, Neuronal, CD325 Antigen, N-Cadherin 1, Cadherin-2, CD325.
Product # :
PRO-2455Price :
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Description
CDH2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 574 amino acids (160-724a.a.) and having a molecular mass of 62.9kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).CDH2 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CDH2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Cadherin-2 isoform 1, also known as CDH2 is a transmembrane, homophilic glycoprotein which belongs to the calcium-dependent cell adhesion molecule family. CDH2 takes part in neurons and later on was discovered to participate in cardiac muscle and in cancer metastasis as well. The CDH2 loss promotes tumorigenesis through releasing membrane-bound β-catenin, and so stimulating Wnt signaling. Furthermore, CDH2 appears to be implicated in tumor development, however this discovery is limited in adrenocortical tumors-ACTs.
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Synonyms
Cadherin 2, Cadherin 2, Type 1, N-Cadherin (Neuronal), Neural Cadherin, N-Cadherin, CDw325, NCAD, CDHN, Calcium-Dependent Adhesion Protein, Neuronal, CD325 Antigen, N-Cadherin 1, Cadherin-2, CD325.
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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
ADPDWVIPPI NLPENSRGPF PQELVRIRSD RDKNLSLRYS VTGPGADQPP TGIFIINPIS GQLSVTKPLD REQIARFHLR AHAVDINGNQ VENPIDIVIN VIDMNDNRPE FLHQVWNGTV PEGSKPGTYV MTVTAIDADD PNALNGMLRY RIVSQAPSTP SPNMFTINNE TGDIITVAAG LDREKVQQYT LIIQATDMEG NPTYGLSNTA TAVITVTDVN DNPPEFTAMT FYGEVPENRV DIIVANLTVT DKDQPHTPAW NAVYRISGGD PTGRFAIQTD PNSNDGLVTV VKPIDFETNR MFVLTVAAEN QVPLAKGIQH PPQSTATVSV TVIDVNENPY FAPNPKIIRQ EEGLHAGTML TTFTAQDPDR YMQQNIRYTK LSDPANWLKI DPVNGQITTI AVLDRESPNV KNNIYNATFL ASDNGIPPMS GTGTLQIYLL DINDNAPQVL PQEAETCETP DPNSINITAL DYDIDPNAGP FAFDLPLSPV TIKRNWTITR LNGDFAQLNL KIKFLEAGIY EVPIIITDSG NPPKSNISIL RVKVCQCDSN GDCTDVDRIV GAGLGTGAHH HHHH.
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 :
HumaninDescription:
Humanin
Product # :
HOR-042Price :
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Description
Humanin Synthetic is a single, non-glycosylated polypeptide chain containing 24 amino acids, having a molecular mass of 2687 Dalton and a Molecular formula of C119H204N34O32S2 .
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
Citations
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Humanin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Humanin 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 Humanin in sterile 18MΩ-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
H-Met-Ala-Pro-Arg-Gly-Phe-Ser-Cys-Leu-Leu-Leu-Leu-Thr-Ser-Glu-Ile-Asp-Leu-Pro-Val-Lys-Arg-Arg-Ala-OH.
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Background
Humanin, a small peptide derived from the mitochondrial genome, has emerged as a remarkable molecule with diverse cellular protective functions. This research paper aims to provide a comprehensive analysis of Humanin, exploring its biochemical properties, mechanisms of action, and potential therapeutic applications in various disease contexts.
Humanin, initially discovered for its role in neuroprotection, has since garnered interest for its broad spectrum of cytoprotective effects. Derived from the mitochondrial 16S ribosomal RNA, this small peptide plays a critical role in safeguarding cells from various stressors (Harvey, 2008). This paper delves into the complexities of Humanin, uncovering its multifaceted nature and potential clinical applications.
Humanin is a 24-amino acid peptide with a unique secondary structure that contributes to its cellular protective functions. It localizes to both the cytoplasm and mitochondria, where it interacts with various proteins involved in apoptotic and oxidative stress pathways (Hoang et al., 2019). Additionally, Humanin can undergo post-translational modifications, further diversifying its actions.
Humanin exerts its protective effects through multiple mechanisms. It interacts with the pro-apoptotic protein Bax, inhibiting its translocation to the mitochondria and preventing the release of cytochrome c (Hashimoto et al., 2001). Humanin also modulates the activities of caspases, key mediators of cell death pathways, thereby promoting cell survival in stressful conditions (Nakagawa et al., 2002).
Beyond its initial recognition as a neuroprotective agent, Humanin has demonstrated cytoprotective effects in various cell types, including cardiomyocytes, neurons, and endothelial cells (Chai et al., 2019). It attenuates oxidative stress, reduces mitochondrial dysfunction, and promotes cell viability, thereby safeguarding cells from a multitude of insults.
The multifaceted protective functions of Humanin offer promising therapeutic potential in various disease contexts. Research has shown its efficacy in mitigating neurodegenerative disorders, cardiovascular diseases, and age-related pathologies (Muzumdar et al., 2009). Furthermore, Humanin's ability to attenuate inflammation and promote tissue repair opens new avenues for therapeutic interventions.
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 :
S100A7 HumanDescription:
S100 Calcium Binding Protein A7 Human Recombinant
S100 calcium-binding protein A7 (psoriasin 1), S100A7c, PSOR1.
Product # :
PRO-149Price :
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Description
S100A7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 121 amino acids (1-101) and having a molecular mass of 13.6 kDa.The S100A4 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
S100A7 protein at 0.5mg/ml in 20mM Tris-HCl, pH-8, 0.1M NaCl, 1mM DTT and 30% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
S100A7 is a member of the S-100 family of calcium binding proteins and is produced through a non-classical secretory pathway to the cytoplasm. S100A7 takes part in the regulation of several cellular courses, such as cell cycle, cell progression and cellular differentiation. S100A7 holds two EF-hand domains and is extremely upregulated in psoriatic epidermis, in addition to bladder squamous cell carcinoma and breast cancer tissue, signifying a probable part in carcinogenesis.
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Synonyms
S100 calcium-binding protein A7 (psoriasin 1), S100A7c, PSOR1.
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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 MSNTQAERSI IGMIDMFHKY TRRDDKIDKP SLLTMMKENFPNFLSACDKK GTNYLADVFE KKDKNEDKKI DFSEFLSLLG DIATDYHKQS HGAAPCSGGS 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 :
CYTH2 HumanDescription:
Cytohesin 2 Human Recombinant
ARF Nucleotide-Binding Site Opener, Pleckstrin Homology Sec7 And Coiled-Coil Domains 2 (Cytohesin-2), PH SEC7 And Coiled-Coil Domain-Containing Protein 2, Cytohesin 2, Protein ARNO, ARF Exchange Factor, Sec7p-Like, PSCD2, PSCD2L, CTS18.1, Sec7p-L, SEC7L.
Product # :
PRO-1248Price :
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Description
CYTH2 Human Recombinant produced in E. coli is a single polypeptide chain containing 422 amino acids (1-399) and having a molecular mass of 48.9 kDa. CYTH2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CYTH2 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Cytohesin 2 (CYTH2) is an ARF-1 guanine nucleotide exchange factor (GEF). ARF (ADP ribosylation factor) proteins are a part of a group within the RAS superfamily and bindes GTP-b proteins central to the process of vesicle budding. CYTH2 promotes guanine-nucleotide exchange on ARF1, ARF3 and ARF6. Furthermore, CYTH2 promotes the activation of ARF factors through replacement of GDP with GTP. The protein encoded by CYTH2 is a member of the PSCD family. Members of PSCD family appear to mediate the regulation of protein sorting and membrane trafficking. The cell membrane form, in association with ARL4 proteins, recruits ARF6 to the plasma membrane.
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Synonyms
ARF Nucleotide-Binding Site Opener, Pleckstrin Homology Sec7 And Coiled-Coil Domains 2 (Cytohesin-2), PH SEC7 And Coiled-Coil Domain-Containing Protein 2, Cytohesin 2, Protein ARNO, ARF Exchange Factor, Sec7p-Like, PSCD2, PSCD2L, CTS18.1, Sec7p-L, SEC7L.
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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 MGSMEDGVYE PPDLTPEERM ELENIRRRKQ ELLVEIQRLR EELSEAMSEV EGLEANEGSK TLQRNRKMAM GRKKFNMDPK KGIQFLVENE LLQNTPEEIA RFLYKGEGLN KTAIGDYLGE REELNLAVLH AFVDLHEFTD LNLVQALRQF LWSFRLPGEA QKIDRMMEAF AQRYCLCNPG VFQSTDTCYV LSFAVIMLNT SLHNPNVRDK PGLERFVAMN RGINEGGDLP EELLRNLYDS IRNEPFKIPE DDGNDLTHTF FNPDREGWLL KLGGRVKTWK RRWFILTDNC LYYFEYTTDK EPRGIIPLEN LSIREVDDPR KPNCFELYIP NNKGQLIKAC KTEADGRVVE GNHMVYRISA PTQEEKDEWI KSIQAAVSVD PFYEMLAARK KRISVKKKQE QP.
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 :
CYTIP HumanDescription:
Cytohesin 1 Interacting Protein Human Recombinant
Cytohesin 1 Interacting Protein, Cytohesin Binder And Regulator, PSCDBP, Pleckstrin Homology, Sec7 And Coiled-Coil Domains, Binding Protein,Pleckstrin Homology Sec7 And Coiled-Coil Domains-Binding Protein, Cytohesin-Associated Scaffolding Protein, Cytohesin Binding Protein HE, Cytohesin-Binding Protein HE, Cbp HE, CASP, CYBR, HE Pleckstrin Homology, Sec7 And Coiled/Coil Domains, Binding Protein, Cytohesin-1 Interacting Protein, Cytohesin-Interacting Protein, CYTHIP, B3-1, CYTIP.
Product # :
PRO-2172Price :
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Description
CYTIP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 384 amino acids (1-359 a.a) and having a molecular mass of 42.6kDa.CYTIP is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CYTIP protein solution (1mg/ml) containing 20mM Tris-HCl (pH 8.0) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Cytohesin-interacting protein, also known as CYTIP contains 2 leucine zipper domains as well as a putative C-terminal nuclear targeting signal. However, CYTIP does not contain any hydrophobic regions. In addition, CYTIP is expressed weakly in resting NK and T cells. It also modulates the activation of ARF genes by CYTH1.
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Synonyms
Cytohesin 1 Interacting Protein, Cytohesin Binder And Regulator, PSCDBP, Pleckstrin Homology, Sec7 And Coiled-Coil Domains, Binding Protein,Pleckstrin Homology Sec7 And Coiled-Coil Domains-Binding Protein, Cytohesin-Associated Scaffolding Protein, Cytohesin Binding Protein HE, Cytohesin-Binding Protein HE, Cbp HE, CASP, CYBR, HE Pleckstrin Homology, Sec7 And Coiled/Coil Domains, Binding Protein, Cytohesin-1 Interacting Protein, Cytohesin-Interacting Protein, CYTHIP, B3-1, CYTIP.
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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 SSGLVPPGSH MGSEFMSLQR LLQHSSNGNL ADFCAGPAYS SYSTLTGSLT MDDNRRIQML ADTVATLPRG RKQLALTRSS SLSDFSWSQR KLVTVEKQDN ETFGFEIQSY RPQNQNACSS EMFTLICKIQ EDSPAHCAGL QAGDVLANIN GVSTEGFTYK QVVDLIRSSG NLLTIETLNG TMILKRTELE AKLQVLKQTL KQKWVEYRSL QLQEHRLLHG DAANCPSLEN MDLDELSLFG PLPGPGPALV DRNRLSSESS CKSWLSSMTM DSEDGYQTCV SEDSSRGAFS RQTSTDDECF IPKEGDDFLR RSSSRRNRSI SNTSSGSMSP LWEGNLSSMF GTLPRKSRKG SVRKQLLKFI PGLHRAVEEE ESRF
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 :
ANXA11 HumanDescription:
Annexin A11 Human Recombinant
Annexin A11, 56 kDa autoantigen, Annexin XI, Annexin-11, Calcyclin-associated annexin 50, CAP-50, ANXA11, ANX11, CAP50.
Product # :
PRO-278Price :
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Description
ANXA11 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 525 amino acids (1-505) and having a molecular mass of 56.6 kDa. The ANXA11 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ANXA11 solution (0.25mg/ml) contains 20mM MES buffer (Ph 5.0), 20% glycerol, 2mM DTT and 100mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Annexin A11 (ANXA11) belongs to the annexin family, which is a group of calcium-dependent phospholipid-binding proteins. Annexins have distinctive N-terminal domains and conserved C-terminal domains, which contain the calcium-dependent phospholipid-binding sites. Annexin A11 binds specifically to calcyclin in a calcium-dependent manner. Moreover, ANXA11 is required for midbody formation and completion of the terminal phase of cytokinesis. The ANXA11 protein is a 56kDa antigen recognized by sera from patients with various autoimmune diseases.
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Synonyms
Annexin A11, 56 kDa autoantigen, Annexin XI, Annexin-11, Calcyclin-associated annexin 50, CAP-50, ANXA11, ANX11, CAP50.
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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 MSYPGYPPPP GGYPPAAPGG GPWGGAAYPP PPSMPPIGLD NVATYAGQFN QDYLSGMAAN MSGTFGGANM PNLYPGAPGA GYPPVPPGGF GQPPSAQQPV PPYGMYPPPG NPPSRMPSY PPYPGAPVPG QPMPPPGQQP PGAYPGQPPV TYPGQPPVPL PGQQQPVPSY PGYPGSGTVT PAVPPTQFGS RGTITDAPGF DPLRDAEVLR KAMKGFGTDE QAIIDCLGSR SNKQRQQILL SFKTAYGKDL IKDLKSELSG NFEKTILALM KTPVLFDIYE IKEAIKGVGT DEACLIEILA SRSNEHIREL NRAYKAEFKK TLEEAIRSDT GHFQRLLIS LSQGNRDEST NVDMSLAQRD AQELYAAGEN RLGTDESKFN AVLCSRSRAH LVAVFNEYQR MTGRDIEKSI CREMSGDLEE GMLAVVKCLK NTPAFFAERL NKAMRGAGTK DRTLIRIMVS RSETDLLDIR SEYKRMYGKS LYHDISGDTS GDYRKILLKI CGGND.
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 :
HSA Fatty Acid freeDescription:
Human Serum Albumin Recombinant, Fatty Acid Free
Serum albumin, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.
Product # :
PRO-1917Price :
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Description
HSA Human Recombinant Fatty Acid reduced produced in Plant contains 585 amino acids having a molecular mass of 67 kDa. The recombinant Albumin is purified by proprietary chromatographic techniques.
Source
Rice Grain.
Formulation
solution containing no additives.
Purity
Greater than 97% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Albumin is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted albumin. Albumin is a soluble, monomeric protein which comprises about one-half of the blood serum protein. Albumin functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume. Mutations in this gene on chromosome 4 result in various anomalous proteins. Albumin is a globular unglycosylated serum protein of molecular weight 65,000. The human albumin gene is 16,961 nucleotides long from the putative 'cap' site to the first poly (A) addition site. It is split into 15 exons which are symmetrically placed within the 3 domains that are thought to have arisen by triplication of a single primordial domain.
HSA is widely used to stabilize -
Synonyms
Serum albumin, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.
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Physical Appearance
Sterile Filtered clear yellowish solution.
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Stability
Recombinant Albumin stable at room temperature for 2 weeks should be stored at 4°C.
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 :
S100A9 MouseDescription:
S100 Calcium Binding Protein A9 Mouse Recombinant
Calgranulin B, 60B8AG, CAGB, CFAG, CGLB, L1AG, LIAG, MAC387, MIF, MRP14, NIF, P14, Protein S100-A9, S100 calcium-binding protein A9.
Product # :
PRO-878Price :
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Description
S100A9 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 133 amino acids (1-113) and having a molecular mass of 15.2 kDa.The S100A9 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
S100A9 protein (0.5mg/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
S100A9 is part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100A9 protein is localized in the cytoplasm and/or nucleus of a wide range of cells, and participates in the regulation of several cellular processes such as cell cycle progression and differentiation. S100 genes include no less than 13 proteins which are localized as a cluster on chromosome 1q21. S100A9 is involved in the inhibition of casein kinase and altered expression of this protein is associated with the disease cystic fibrosis.
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Synonyms
Calgranulin B, 60B8AG, CAGB, CFAG, CGLB, L1AG, LIAG, MAC387, MIF, MRP14, NIF, P14, Protein S100-A9, S100 calcium-binding protein A9.
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Physical Appearance
S100A9 is supplied as a sterile filtered yellowish 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 MANKAPSQME RSITTIIDTF HQYSRKEGHP DTLSKKEFRQ MVEAQLATFM KKEKRNEALI NDIMEDLDTN QDNQLSFEEC MMLMAKLIFA CHEKLHENNP RGHGHSHGKG CGK
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 :
Omentin HumanDescription:
Omentin Human Recombinant
Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.
Product # :
CYT-301Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Omentin Human Recombinant is produced in E.Coli by recombinant DNA technology is a single, polypeptide chain containing 313 amino acids and having a molecular mass of 35 kDa. Intelectin is purified by proprietary chromatographic techniques.
Source
E.Coli.
Formulation
Each mg of lyophilized powder contains 10mM NaP, pH-7.5 and 5:1 mannitol to protein.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Omentin is a recently recognized gene highly localized to the mental tissue (visceral adipose tissue). Omentin is present in the stromal vascular cells in the adipose tissue rather than in the adipocytes. Omentin is predominantly expressed in the visceral adipose tissue than the subcutaneous tissue, with the omentin mRNA being 150 times higher in the visceral adipose tissue. Omentin has also been detected in human blood using western blot analysis, and seems to increase INSstimulated glucose uptake in 3T3-L1 adipocytes in mice. Omentin seems to increase Akt phosphorylation irrespective of INS presence. Its role in glucose metabolism and obesity remains to be described; an INS-sensitizing action is possible.Differences in Omentin expression has been noted in adipose tissue from normals and patients with inflammatory bowel disease although its significance is unknown.
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Synonyms
Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Intelectin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Intelectin 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 Omentin 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
MNQLSFLLFL IATTRGWSTD EANTYFKEWTCSSSPSLPRS CKEIKDECPS AFDGLYFLRT ENGVIYQTFC DMTSGGGGWT LVASVHENDM RGKCTVGDRW SSQQGSKADY PEGDGNWANY NTFGSAEAAT SDDYKNPGYY DIQAKDLGIW HVPNKSPMQH WRNSSLLRYR TDTGFLQTLG HNLFGIYQKY PVKYGEGKCW TDNGPVIPVV YDFGDAQKTA SYYSPYGQRE FNNERAANAL CAGMRVTGCN TEHHCIGGGG YFPEASPQQC GDFSGFDWSG YGTHVGYSSS REITEAAVLLFYR.
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 :
KLF4 HumanDescription:
Kruppel-Like Factor 4 Human Recombinant
Kruppel-like factor 4 (gut), EZF, GKLF, Epithelial zinc finger protein EZF, Gut-enriched krueppel-like factor, endothelial Kruppel-like zinc finger protein.
Product # :
PRO-891Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
KLF4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 545 amino acids (11-395) and having a molecular mass of 58.1 kDa.The KLF4 is fused to a 159 amino acid His-CaM Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The KLF4 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
KLF4 is a transcription factor that performs as both an activator and repressor. KLF4 is expressed mainly in erythroid tissues and found mostly in gut. KLF4 is takes part in the differentiation of epithelial cells in addition to skeletal and kidney development.
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Synonyms
Kruppel-like factor 4 (gut), EZF, GKLF, Epithelial zinc finger protein EZF, Gut-enriched krueppel-like factor, endothelial Kruppel-like zinc finger protein.
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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
MAHHHHHHMA DQLTEEQIAE FKEAFSLFDK DGDGTITTKE LGTVMRSLGQ NPTEAELQDM INEVDADGNG TIDFPEFLTM MARKMKDTDS EEEIREAFRV FDKDGNGYIS AAELRHVMTN LGEKLTDEEV DEMIREADID GDGQVNYEEF VQMMTAKGSM AVSDALLPSF STFASGPAGR EKTLRQAGAP NNRWREELSH MKRLPPVLPG RPYDLAAATV ATDLESGGAG AACGGSNLAP LPRRETEEFN DLLDLDFILS NSLTHPPESV AATVSSSASA SSSSSPSSSG PASAPSTCSF TYPIRAGNDP GVAPGGTGGG LLYGRESAPP PTAPFNLADI NDVSPSGGFV AELLRPELDP VYIPPQQPQP PGGGLMGKFV LKASLSAPGS EYGSPSVISV SKGSPDGSHP VVVAPYNGGP PRTCPKIKQE AVSSCTHLGA GPPLSNGHRP AAHDFPLGRQ LPSRTTPTLG LEEVLSSRDC HPALPLPPGF HPHPGPNYPS FLPDQMQPQV PPLHYQELMP PGSCMPEEPK PKRGRRSWPR KRTAT
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 :
ATF HumanDescription:
Apo Transferrin Human
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.
Product # :
PRO-325Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Human Apo Transferrin is a glycoprotein of approximately 77 kDa.
Source
Human serum.
Formulation
The protein was lyophilized from 20mM NH4HC03 solution. May contain traces of buffer salts.
Purity
Greater than 98.0% as determined by coomassie blue stained SDS-PAGE and Cellulose Acetate electrophoresis.
Citations
More Info
-
Introduction
Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
Human Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Human Transferrin is Critical for long-term cells growth in-vitro. Human Transferrin is used as detoxificant in media by binding contaminating metal ions. Human Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Human Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells. -
Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store the lyophilized Apo Transferrin between 2-8°C, do not freeze. Upon reconstitution Apo Transferrin 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 Apo Transferrin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV, HBSAG and Syphilis.
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Iron Content
The Iron content was estimated by ICP and was found to be <6 ppm.
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 :
DCN MouseDescription:
Decorin Mouse Recombinant
Decorin, Bone proteoglycan II, PG-S2, PG40, DCN.
Product # :
PRO-2234Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DCN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (17-354 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 344 amino acids and having a molecular mass of 38.8kDa.DCN shows multiple bands between 40-57kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
DCN protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4), 30% glycerol and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Decorin (DCN) is a small cellular or pericellular matrix proteoglycan which is closely related in structure to biglycan protein. Decorin is a secreted protein which binds to collagen and fibronectin in extracellular matrix. Decorin appears in different glycoforms, substituted with chondroitin sulfate or dermatan sulfate consistent with the original tissue. DCN contains one attached glycosaminoglycan chain. Decorin influences the rate of fibril formation. Decorin is capable of suppressing the growth of various tumor cell lines. DCN gene defects cause corneal dystrophy. The DCN gene is a candidate gene for Marfan syndrome.
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Synonyms
Decorin, Bone proteoglycan II, PG-S2, PG40, DCN.
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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
GPFEQRGLFD FMLEDEASGI IPYDPDNPLI SMCPYRCQCH LRVVQCSDLG LDKVPWDFPP DTTLLDLQNN KITEIKEGAF KNLKDLHTLI LVNNKISKIS PEAFKPLVKL ERLYLSKNQL KELPEKMPRT LQELRVHENE ITKLRKSDFN GLNNVLVIEL GGNPLKNSGI ENGAFQGLKS LSYIRISDTN ITAIPQGLPT SLTEVHLDGN KITKVDAPSL KGLINLSKLG LSFNSITVME NGSLANVPHL RELHLDNNKL LRVPAGLAQH KYIQVVYLHN NNISAVGQND FCRAGHPSRK ASYSAVSLYG NPVRYWEIFP NTFRCVYVRS AIQLGNYKHH HHHH
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 :
PFDN6 HumanDescription:
Prefoldin Subunit 6 Human Recombinant
Prefoldin Subunit 6, PFD6, H2-KE2, KE-2, HKE2, HLA class II region expressed gene KE2, MGC70744.
Product # :
PRO-178Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PFDN6 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 149 amino acids (1-129a.a.) and having a molecular mass of 16.7 kDa. PFDN6 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PFDN6 protein solution (0.5mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH8.0), 100mM NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
PFDN6 is a subunit of the heteromeric prefoldin complex that chaperones developing actin and alpha- and beta-tubulin chains until they are transferred to the cytosolic chaperonin containing TCP1 (CCT) complex. PFDN6 binds specifically to cytosolic chaperonin (c-CPN), transfers target proteins to it and bind to developing polypeptide chain to promote folding in a setting where there are many competing pathways for nonnative proteins.
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Synonyms
Prefoldin Subunit 6, PFD6, H2-KE2, KE-2, HKE2, HLA class II region expressed gene KE2, MGC70744.
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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 MAELIQKKLQ GEVEKYQQLQ KDLSKSMSGR QKLEAQLTEN NIVKEELALL DGSNVVFKLL GPVLVKQELG EARATVGKRL DYITAEIKRY ESQLRDLERQ SEQQRETLAQ LQQEFQRAQA AKAGAPGKA
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 :
FZD4 HumanDescription:
Frizzled Class Receptor 4 Human Recombinant
Frizzled-4, Fz-4, hFz4, FzE4, CD344, FZD4.
Product # :
PRO-2464Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
FZD4 Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 428 amino acids (37-222 a.a.) and having a molecular mass of 48.3kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). FZD4 is expressed with a 239 amino acids hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
FZD4 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
-
Introduction
Frizzled-4, also known as FZD4 is a 7 transmembrane glycoprotein which belongs to the Frizzled family within the G-protein coupled receptor superfamily. FZD4 acts as a positive regulator of the Wingless type MMTV integration site signaling pathway. These pathways appear to include interactions with G-proteins. FZD4 is implicated in transduction as well as intercellular transmission of polarity information in the course of tissue morphogenesis and differentiated tissues.
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Synonyms
Frizzled-4, Fz-4, hFz4, FzE4, CD344, FZD4.
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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
ADPFGDEEER RCDPIRISMC QNLGYNVTKM PNLVGHELQT DAELQLTTFT PLIQYGCSSQ LQFFLCSVYV PMCTEKINIP IGPCGGMCLS VKRRCEPVLK EFGFAWPESL NCSKFPPQND HNHMCMEGPG DEEVPLPHKT PIQPGEECHS VGTNSDQYIW VKRSLNCVLK CGYDAGLYSR
SAKEFTDIWL EPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG
QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GKHHHHHH
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 :
HAPLN1 HumanDescription:
Hyaluronan And Proteoglycan Link Protein 1 Human Recombinant
Hyaluronan and proteoglycan link protein 1 precursor, CRTL1, Cartilage-linking protein 1, Cartilage-link protein, Proteoglycan link protein, HAPLN1.
Product # :
PRO-2012Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HAPLN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 362 amino acids (16-354 a.a.) and having a molecular mass of 40.9kDa.HAPLN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HAPLN1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Hyaluronan And Proteoglycan Link Protein 1, which is also known as HAPLN1 is a part of the HAPLN family.HAPLN1 contains one Ig-like V-type domain and two Link domains. In the extracellular cartilage matrix, HAPLN1 stabilizes the aggregates of proteoglycan monomers by means of hyaluronic acid .
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Synonyms
Hyaluronan and proteoglycan link protein 1 precursor, CRTL1, Cartilage-linking protein 1, Cartilage-link protein, Proteoglycan link protein, HAPLN1.
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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 MGSDHLSDNY TLDHDRAIHI QAENGPHLLV EAEQAKVFSH RGGNVTLPCK FYRDPTAFGS GIHKIRIKWT KLTSDYLKEV DVFVSMGYHK KTYGGYQGRV FLKGGSDSDA SLVITDLTLE DYGRYKCEVI EGLEDDTVVV ALDLQGVVFP YFPRLGRYNL NFHEAQQACL DQDAVIASFD QLYDAWRGGL DWCNAGWLSD GSVQYPITKP REPCGGQNTV PGVRNYGFWD KDKSRYDVFC FTSNFNGRFY YLIHPTKLTY DEAVQACLND GAQIAKVGQI FAAWKILGYD RCDAGWLADG SVRYPISRPR RRCSPTEAAV RFVGFPDKKH KLYGVYCFRA YN.
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 :
S100A7A HumanDescription:
S100 Calcium Binding Protein A7A Human Recombinant
NICE-2, NICE2, Protein S100-A7A, S100A15, S100A7f, S100A7L1, S100 calcium-binding protein A15, S100 calcium-binding protein A7A, S100 calcium-binding protein A7-like 1, S100A7A.
Product # :
PRO-756Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The S100A7A Human Recombinant is manufactured with N-terminal fusion of 9 amino acids His Tag. The S100A7A His -Tagged Fusion Protein is a 12.3kDa protein containing 109 amino acid residues and 9 additional amino acid residues - His Tag (underlined).
Source
Escherichia Coli.
Formulation
Filtered and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl pH-7.5.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
S100A7A takes part in epidermal differentiation and inflammation thus is significant for the pathogenesis of psoriasis and other diseases.
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Synonyms
NICE-2, NICE2, Protein S100-A7A, S100A15, S100A7f, S100A7L1, S100 calcium-binding protein A15, S100 calcium-binding protein A7A, S100 calcium-binding protein A7-like 1, S100A7A.
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Stability
Store lyophilized S100A7A Human recombinant at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted S100A7A 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
Add pyrogen free water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. Product 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
MMKHHHHHHASNTQAERSIIG MIDMFHKYTG RDGKIEKPSL LTMMKENFPN FLSACDKKGI HYLATVFEKK DKNEDKKIDF SEFLSLLGDI AADYHKQSHG AAPCSGGSQ.
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 :
ACVRL1 HumanDescription:
Activin A Receptor Type II-Like 1 Human Recombinant
Activin A Receptor Type II-Like 1, ACVRLK1, ALK1, TGF-B Superfamily Receptor Type I EC 2.7.11.30, TSR-I, ALK-1, HHT2, SKR3 Serine/Threonine-Protein Kinase Receptor R3 Activin A Receptor, Type II-Like Kinase 1, Activin Receptor-Like Kinase 1, EC 2.7.11, ORW2, HHT.
Product # :
CYT-920Price :
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Shipped with Ice Packs
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Description
ACVRL1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 103 amino acids (22-118a.a.) and having a molecular mass of 11.5kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).ACVRL1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
ACVRL1 protein solution (0.25mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Synonyms
Activin A Receptor Type II-Like 1, ACVRLK1, ALK1, TGF-B Superfamily Receptor Type I EC 2.7.11.30, TSR-I, ALK-1, HHT2, SKR3 Serine/Threonine-Protein Kinase Receptor R3 Activin A Receptor, Type II-Like Kinase 1, Activin Receptor-Like Kinase 1, EC 2.7.11, ORW2, HHT.
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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
DPVKPSRGPL VTCTCESPHC KGPTCRGAWC TVVLVREEGR HPQEHRGCGN LHRELCRGRP TEFVNHYCCD SHLCNHNVSL VLEATQPPSEQPGTDGQHHH HHH.
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Background
The Physiological Implications and Therapeutic Potential of Activin A Receptor Type II-Like 1 Human Recombinant
1. Abstract
This research paper investigates the Activin A Receptor Type II-Like 1 Human Recombinant (ACVRL1), a significant protein involved in the TGF-beta superfamily signaling pathway. We provide an extensive understanding of ACVRL1’s structure, signaling mechanism, biological functions, and implications in disease pathology. Additionally, we explore the therapeutic potential of ACVRL1 in various pathological conditions.
2. Introduction
ACVRL1, also known as ALK1, plays an essential role in the TGF-beta signaling pathway, which has implications in cellular proliferation, differentiation, and apoptosis. Understanding ACVRL1 and its signaling mechanisms could provide insights into its potential therapeutic applications in various diseases.
3. Structure and Signaling of ACVRL1
ACVRL1 is a type I receptor protein involved in the TGF-beta signaling pathway. It is a transmembrane protein that consists of a ligand-binding extracellular domain and an intracellular domain responsible for signal transduction. Binding of ligands to ACVRL1 triggers phosphorylation events that activate downstream signaling pathways.
4. Biological Functions of ACVRL1
ACVRL1 plays pivotal roles in multiple biological processes, including vascular development, angiogenesis, and maintenance of vascular integrity. It is known to influence cellular processes such as proliferation, differentiation, and apoptosis, thereby implicating it in organogenesis and homeostasis.
5. ACVRL1 in Disease Pathology
Mutations in the ACVRL1 gene have been associated with hereditary hemorrhagic telangiectasia (HHT), a genetic disorder characterized by abnormal blood vessel formation. This link underscores the critical role of ACVRL1 in vascular biology and disease.
6. Therapeutic Potential of ACVRL1
Given its crucial role in vascular biology and its link to HHT, ACVRL1 presents a promising target for therapeutic interventions. Modulation of ACVRL1 signaling could potentially provide treatment options for pathological conditions related to abnormal blood vessel formation and function.
7. Conclusion and Future Perspectives
Our understanding of ACVRL1 and its functions has grown significantly in recent years, but there is much yet to be discovered. Continued research into ACVRL1's precise molecular mechanisms and its roles in disease will undoubtedly open new doors for therapeutic developmen
What is the molecular weight / Mw of ACVRL1 Protein?
ACVRL1 Protein has a total Mw of 11.5kDa.What is the source or expression system of ACVRL1 Protein?
Sf9, Insect cells.
What is the Purity of ACVRL1 Protein?
ACVRL1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ACVRL1 Protein?
The biological functionality of ACVRL1 Protein will be determined in the future.
What is the amino acid sequence of ACVRL1 Protein?
DPVKPSRGPL VTCTCESPHC KGPTCRGAWC TVVLVREEGR HPQEHRGCGN LHRELCRGRP TEFVNHYCCD SHLCNHNVSL VLEATQPPSEQPGTDGQHHH HHH.
What applications can ACVRL1 Protein be used in?
ACVRL1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ACVRL1 Protein?
The endotoxin level is minimal, ACVRL1 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 :
CTSA MouseDescription:
Cathepsin-A Mouse Recombinant
Lysosomal protective protein (EC:3.4.16.5), Carboxypeptidase C, Carboxypeptidase, Cathepsin A, Protective protein cathepsin A, PPCA, Protective protein for beta-galactosidase.
Product # :
ENZ-945Price :
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Shipped with Ice Packs
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Description
CTSA produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 459 amino acids (24-474 a.a.) and having a molecular mass of 52.4kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).CTSA is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9 Insect cells.
Formulation
CTSA protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Cathepsin-A (CTSA) is a protective protein which is crucial for both the activity of beta-galactosidase and neuraminidase, CTSA associates with these enzymes and exerts a protective function required for their stability and activity. The CTSA protein is also a carboxypeptidase and can deamidate tachykinins. CTSA is a component of the lysosomal multienzyme complex along with beta-galactosidase and sialidase Neu1. CTSA is a multicatalytic enzyme with deamidase and esterase in addition to carboxypeptidase activities.
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Synonyms
Lysosomal protective protein (EC:3.4.16.5), Carboxypeptidase C, Carboxypeptidase, Cathepsin A, Protective protein cathepsin A, PPCA, Protective protein for beta-galactosidase.
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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
APDQDEIDCL PGLAKQPSFR QYSGYLRASD SKHFHYWFVE SQNDPKNSPV VLWLNGGPGC SSLDGLLTEH GPFLIQPDGV TLEYNPYAWN LIANVLYIES PAGVGFSYSD DKMYVTNDTE VAENNYEALK DFFRLFPEYK DNKLFLTGES YAGIYIPTLA VLVMQDPSMN LQGLAVGNGL ASYEQNDNSL VYFAYYHGLL GNRLWTSLQT HCCAQNKCNF YDNKDPECVN NLLEVSRIVG KSGLNIYNLY APCAGGVPGR HRYEDTLVVQ DFGNIFTRLP LKRRFPEALM RSGDKVRLDP PCTNTTAPSN YLNNPYVRKA LHIPESLPRW DMCNFLVNLQ YRRLYQSMNS QYLKLLSSQK YQILLYNGDV DMACNFMGDE WFVDSLNQKM EVQRRPWLVD YGESGEQVAG FVKECSHITF LTIKGAGHMV PTDKPRAAFT MFSRFLNKEP YVEHHHHHH.
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 :
HPCAL1 HumanDescription:
Hippocalcin-Like 1 Human Recombinant
Hippocalcin-Like 1, HLP2, BDR1, Calcium-Binding protein BDR-1, Visinin-Like protein 3, VILIP-3
Product # :
PRO-254Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HPCAL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213amino acids (1-193a.a.) and having a molecular wieght of 24.4kDa. The HPCAL1 is fused to 20a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HPCAL1 protein solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH8.0) containing 1mM DTT 0.2M NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
HPCAL1, participates in neuron-specific calcium-binding proteins family found in the retina and brain. HPCAL1 is extremely comparable to human hippocalcin protein and almost equal to the rat and mouse hippocalcin like-1 proteins. HPCAL1 takes part in the calcium-dependent regulation of rhodopsin phosphorylation and can have importance in neuronal signalling in the central nervous system.
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Synonyms
Hippocalcin-Like 1, HLP2, BDR1, Calcium-Binding protein BDR-1, Visinin-Like protein 3,
VILIP-3 -
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 MGKQNSKLRP EVLQDLRENT EFTDHELQEW YKGFLKDCPT GHLTVDEFKK IYANFFPYGD ASKFAEHVFR TFDTNGDGTI DFREFIIALS VTSRGKLEQK LKWAFSMYDL DGNGYISRSE MLEIVQAIYK MVSSVMKMPE DESTPEKRTD KIFRQMDTNN DGKLSLEEFI RGAKSDPSIV RLLQCDPSSA SQF
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 :
SOST MouseDescription:
Sclerostin Mouse Recombinant
SOST, Sclerostin, 5430411E23Rik.
Product # :
PRO-2670Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SOST Mouse Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (24-211 a.a) containing 194 amino acids and having a molecular mass of 21.9 kDa.SOST is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
SOST protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Sclerostin (SOST) is a secreted glycoprotein with a C-terminal cysteine knot-like (CTCK) domain and sequence similarity to the DAN (differential screening-selected gene aberrative in neuroblastoma) family of bone morphogenetic protein antagonists. Sclerostin functions as a negative regulator of bone growth, by inhibiting bone formation. SOST is expressed mainly in the bone, cartilage, kidney, liver, bone marrow and primary osteoblasts differentiated for 21 days. SOST gene defects cause sclerosteosis and bone dysplasia.
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Synonyms
SOST, Sclerostin, 5430411E23Rik.
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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
QGWQAFRNDA TEVIPGLGEY PEPPPENNQT MNRAENGGRP PHHPYDAKDV SEYSCRELHY TRFLTDGPCR SAKPVTELVC SGQCGPARLL PNAIGRVKWW RPNGPDFRCI PDRYRAQRVQ LLCPGGAAPR SRKVRLVASC KCKRLTRFHN QSELKDFGPE TARPQKGRKP RPGARGAKAN QAELENAYHH HHHH
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 :
STMN3 HumanDescription:
Stathmin Like-3 Human Recombinant
Stathmin-3, SCG10-like protein, STMN3, SCLIP
Product # :
PRO-838Price :
Quantity :
Shipping Method :
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Description
STMN3 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (39-180 a.a.) and having a molecular mass of 18.9 kDa. The STMN3 is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
STMN3 Human solution containing 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
STMN3 is a neuronal specific protein which belongs to the stathmin/oncoprotein 18 family of microtubule-destabilizing phosphoproteins. It is similar to the SCG10 protein and is involved in signal transduction and regulation of microtubule dynamics.
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Synonyms
Stathmin-3, SCG10-like protein, STMN3, SCLIP
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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 MDMEVKQLDK RASGQSFEVI LKSPSDLSPE SPMLSSPPKK KDTSLEELQK RLEAAEERRK TQEAQVLKQL AERREHEREV LHKALEENNN FSRQAEEKLN YKMELSKEIR EAHLAALRER LREKELHAAE VRRNKEQREE MSG.
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 :
Calumenin HumanDescription:
Calumenin Human Recombinant
CALU, Crocalbin, IEF SSP 9302, FLJ90608, Calumenin.
Product # :
PRO-2465Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Calumenin Human Recombinant produced in E. coli is a single polypeptide chain containing 297 amino acids (20-315) and having a molecular mass of 35kDa. Calumenin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Calumenin solution (0.5mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The IC50 value is < 2.0nM. The inhibitory function of Cystatin 5 on protease activity of papain was measured by a fluorometric assay using Z-FR-AMC at pH 7.5 at 25C.Citations
More Info
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Introduction
Calumenin is a calcium-binding protein located in the endoplasmic reticulum (ER) and sarcoplasmic reticulum (SR) of mammalian tissues which plays a role in ER functions as protein folding and sorting. Calumenin belongs to a family of multiple EF-hand proteins (CERC) that include reticulocalbin, ERC-55, and Cab45 and the product of this gene. Calumenin binds 7 calcium ions having low affinity and takes part in such ER functions as protein folding and sorting.
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Synonyms
CALU, Crocalbin, IEF SSP 9302, FLJ90608, Calumenin.
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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
MKPTEKKDRV HHEPQLSDKV HNDAQSFDYD HDAFLGAEEA KTFDQLTPEE SKERLGKIVS KIDGDKDGFV TVDELKDWIK FAQKRWIYED VERQWKGHDL NEDGLVSWEE YKNATYGYVL DDPDPDDGFN YKQMMVRDER RFKMADKDGD LIATKEEFTA FLHPEEYDYM KDIVVQETME DIDKNADGFI DLEEYIGDMY SHDGNTDEPE WVKTEREQFV EFRDKNRDGK MDKEETKDWI LPSDYDHAEA EARHLVYESD QNKDGKLTKE EIVDKYDLFV GSQATDFGEA LVRHDEF.
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.