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1000 results found for “Vimentin”
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Name :
COMMD6 HumanDescription:
COMM Domain Containing 6 Human Recombinant
COMM domain-containing protein 6, COMM Domain Containing 6, COMMD6, MSTP076, COMM domain-containing protein 6 isoform b, Acrg.
Product # :
PRO-2052Price :
Quantity :
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Shipped with Ice Packs
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Description
COMMD6 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 108 amino acids (1-85) and having a molecular mass of 12kDa.COMMD6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The COMMD6 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 20% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
COMM Domain Containing (COMMD6) which is a part of the NF-kappa-B -inhibiting proteins, contains one COMM domain. COMMD6 down-regulates the activation of NF-kappa-B and inhibits TNF-induced NFKB1 activation.
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Synonyms
COMM domain-containing protein 6, COMM Domain Containing 6, COMMD6, MSTP076, COMM domain-containing protein 6 isoform b, Acrg.
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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 MGSMEASSEP PLDAKSDVTN QLVDFQWKLG MAVSSDTCRS LKYPYVAVML KVADHSGQVK TKCFEMTIPQ FQNFYRQFKE IAAVIETV.
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 :
MCM7 HumanDescription:
Minichromosome Maintenance Complex Component 7 Human Recombinant
Minichromosome Maintenance Complex Component 7, MCM7 Minichromosome Maintenance Deficient 7 (S. Cerevisiae), Minichromosome Maintenance Deficient (S. Cerevisiae) 7, DNA Replication Licensing Factor MCM7, Homolog of S. Cerevisiae Cdc47, CDC47 Homolog, P1CDC47, PNAS146, P85MCM, MCM2, CDC47, P1.1-MCM3, EC 3.6.4.12.
Product # :
PRO-1847Price :
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Description
MCM7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 437 amino acids (1-414) and having a molecular mass of 48.6 kDa. MCM7 is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The MCM7 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
MCM7 is a highly conserved mini-chromosome maintenance protein (MCM) vital for eukaryotic genome replication initiation. The MCM proteins form a hexameric protein complex which is a key component of the pre-replication complex (pre_RC) which takes part in replication forks formation and in DNA replication related proteins recruitment. The MCM complex is comprised of MCM2, 4, 6 and 7 proteins and possesses DNA helicase activity, such as DNA unwinding.
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Synonyms
Minichromosome Maintenance Complex Component 7, MCM7 Minichromosome Maintenance Deficient 7 (S. Cerevisiae), Minichromosome Maintenance Deficient (S. Cerevisiae) 7, DNA Replication Licensing Factor MCM7, Homolog of S. Cerevisiae Cdc47, CDC47 Homolog, P1CDC47, PNAS146, P85MCM, MCM2, CDC47, P1.1-MCM3, EC 3.6.4.12.
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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 MGSMVVATYT CDQCGAETYQ PIQSPTFMPL IMCPSQECQT NRSGGRLYLQ TRGSRFIKFQ EMKMQEHSDQ VPVGNIPRSI TVLVEGENTR IAQPGDHVSV TGIFLPILRT GFRQVVQGLL SETYLEAHRI VKMNKSEDDE SGAGELTREE LRQIAEEDFY EKLAASIAPE IYGHEDVKKA LLLLLVGGVD QSPRGMKIRG NINICLMGDP GVAKSQLLSY IDRLAPRSQY TTGRGSSGVG LTAAVLRDSV SGELTLEGGA LVLADQGVCC IDEFDKMAEA DRTAIHEVME QQTISIAKAG ILTTLNARCS ILAAANPAYG RYNPRRSLEQ NIQLPAALLS RFDLLWLIQD RPDRDNDLRL AQHITYVHQH SRQPPSQFEP LDMKLMRRYI AMCREKQPMV PESLADYITA AYVEMRR
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 :
WNT3A HumanDescription:
Wingless-Type MMTV Integration Site Family, Member 3A Human Recombinant
Protein Wnt-3a, MGC119418, MGC119419, MGC119420, WNT3A, wingless-type MMTV integration site family member 3A.
Product # :
CYT-861Price :
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Description
WNT3A Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 335 amino acids (19-352 a.a.) and having a molecular mass of 37.5kDa. The WNT3A Human is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The WNT3A Human protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
The WNT gene family consists of structurally related genes that encode secreted signaling proteins. These proteins are implicated in oncogenesis and in several developmental processes, including regulation of cell fate and patterning during embryogenesis. WNT3A is a member of the WNT gene family. WNT3A is a protein which shows 96% amino acid identity to mouse Wnt3A protein, and 84% to human WNT3 protein, another WNT gene product. The WNT3A gene is clustered with WNT14 gene, another family member, in chromosome 1q42 region.
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Synonyms
Protein Wnt-3a, MGC119418, MGC119419, MGC119420, WNT3A, wingless-type MMTV integration site family member 3A.
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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
MSYPIWWSLA VGPQYSSLGS QPILCASIPG LVPKQLRFCR NYVEIMPSVA EGIKIGIQEC QHQFRGRRWN CTTVHDSLAI FGPVLDKATR ESAFVHAIAS AGVAFAVTRS CAEGTAAICG CSSRHQGSPG KGWKWGGCSE DIEFGGMVSR EFADARENRP DARSAMNRHN NEAGRQAIAS HMHLKCKCHG LSGSCEVKTC WWSQPDFRAI GDFLKDKYDS ASEMVVEKHR ESRGWVETLR PRYTYFKVPT ERDLVYYEAS PNFCEPNPET GSFGTRDRTC NVSSHGIDGC DLLCCGRGHN ARAERRREKC RCVFHWCCYV SCQECTRVYD VHTCK.
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 :
REN HumanDescription:
Renin Human Recombinant
Renin, Angiotensinogenase, EC 3.4.23.15, HNFJ2, Angiotensin-Forming Enzyme, Renin Precursor Renal, EC 3.4.23.
Product # :
PRO-1529Price :
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Description
REN Human Recombinant produced in E. coli is a single polypeptide chain containing 365 amino acids (67-406) and having a molecular mass of 39.9kDa. REN is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The REN solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
Renin is a highly specific endopeptidase which generates angiotensin I from angiotensinogen in the plasma. angiotensin I is an important regulator of blood pressure and electrolyte balance. Renin initiates a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney.
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Synonyms
Renin, Angiotensinogenase, EC 3.4.23.15, HNFJ2, Angiotensin-Forming Enzyme, Renin Precursor Renal, EC 3.4.23.
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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 MGSHMLTLGN TTSSVILTNY MDTQYYGEIG IGTPPQTFKV VFDTGSSNVW VPSSKCSRLY TACVYHKLFD ASDSSSYKHN GTELTLRYST GTVSGFLSQD IITVGGITVT QMFGEVTEMP ALPFMLAEFD GVVGMGFIEQ AIGRVTPIFD NIISQGVLKE DVFSFYYNRD SENSQSLGGQ IVLGGSDPQH YEGNFHYINL IKTGVWQIQM KGVSVGSSTL LCEDGCLALV DTGASYISGS TSSIEKLMEA LGAKKRLFDY VVKCNEGPTL PDISFHLGGK EYTLTSADYV FQESYSSKKL CTLAIHAMDI PPPTGPTWAL GATFIRKFYT EFDRRNNRIG FALAR.
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 :
IFN tau OvineDescription:
IFN-Tau Ovine Recombinant
IFN-tau1, Trophoblast protein 1, TP-1, Trophoblastin, Antiluteolysin, Trophoblast antiluteolytic protein, IFN-tau, IFN tau-1.
Product # :
CYT-377Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IFN-Tau Ovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 172 amino acids and having a molecular mass of 19914.7 Dalton.The IFN-Tau is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from (1mg/ml) solution containing PBS pH-7.4.
Purity
Greater than 95.0% as determined by both:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 10,000,000IU/mg.More Info
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Introduction
IFN-tau is also known as TP-1 (trophoblast protein-1) is a new class of type I IFN that is secreted by the trophoblast and is the signal for maternal recognition of pregnancy in sheep. IFN- tau has potent immunosuppressive and antiviral activities similar to other type I IFN but is less cytotoxic than IFN-alpha and IFN-beta. The current investigation concerns the effect of recombinant ovine IFN- tau (rOIFN- tau) on the modulation of MHC class I and II expression on cloned mouse cerebrovascular endothelial (CVE) cells.
IFN-tau induced tyrosine phosphorylation of Stat1 and upregulated the expression of MHC class I on CVE. One proposed action by which type I IFN reduces the relapse rate in MS is via interference with IFN-?-induced MHC class II expression. IFN- tau was shown to downregulate IFN-?-induced MHC class II expression on CVE and, hence, may be of potential therapeutic value in downregulating inflammation in the central nervous system (CNS). IFN- tau did not upregulate the expression of MHC class II on CVE. IFN- tau also inhibited the replication of Theiler's virus in CVE. -
Synonyms
IFN-tau1, Trophoblast protein 1, TP-1, Trophoblastin, Antiluteolysin, Trophoblast antiluteolytic protein, IFN-tau, IFN tau-1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IFN-Tau although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-Tau 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 IFN Tau in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Cys-Tyr-Leu-Ser-Arg.
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Background
What is the molecular weight/Mw of IFN TAU OVINE Protein?
IFN TAU OVINE Protein has a total Mw of 19.9kDa.
What is the source or expression system of IFN TAU OVINE Protein?
Escherichia Coli.
What is the Purity of IFN TAU OVINE Protein?
IFN TAU OVINE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IFN TAU OVINE Protein?
The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 10,000,000IU/mg.
What is the amino acid sequence of IFN TAU OVINE Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Cys-Tyr-Leu-Ser-Arg.
What applications can IFN TAU OVINE Protein be used in?
IFN TAU OVINE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFN TAU OVINE Protein?
The endotoxin level is minimal, IFN TAU OVINE 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 :
Eotaxin RatDescription:
Eotaxin Rat Recombinant (CCL11)
Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11.
Product # :
CHM-260Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Eotaxin Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 74 amino acids and having a molecular mass of 8.4kDa. The CCL11 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in in 1×PBS, pH7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract purified blood eosinophils using a concentration range of 0.1-1.0 ug/ml, corresponding to a Specific Activity of 10-100IU/mg.More Info
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Introduction
Chemokine (C-C motif) ligand 11 (CCL11) is a small cytokine belonging to the CC chemokine family that is also known as eotaxin. CCL11 selectively recruits eosinophils by inducing their chemotaxis, and therefore, is implicated in allergic responses. The effects of CCL11 are mediated by its binding to a G-protein-linked receptor known as a chemokine receptor. Chemokine receptors for which CCL11 is a ligand include CCR2, CCR3 and CCR5. The gene for human CCL11 (scya11) is encoded on three exons and is located on chromosome 17.
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Synonyms
Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Eotaxin although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution CCL11 should be stored at 4C between 2-7 days and for future use below -18C.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 Eotaxin 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
HPGSIPTSCC FTMTSKKIPN TLLKSYKRIT NNRCTLKAIV FKTKLGKEICADPKKKWVQD ATKHLDQKLQ TPKP.
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Background
What is the molecular weight/Mw of EOTAXIN RAT Protein?
EOTAXIN RAT Protein has a total Mw of 8.4kDa.
What is the source or expression system of EOTAXIN RAT Protein?
Escherichia Coli.
What is the Purity of EOTAXIN RAT Protein?
EOTAXIN RAT Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of EOTAXIN RAT Protein?
Determined by its ability to chemoattract purified blood eosinophils using a concentration range of 0.1-1.0 ug/ml, corresponding to a Specific Activity of 10-100IU/mg.
What is the amino acid sequence of EOTAXIN RAT Protein?
HPGSIPTSCC FTMTSKKIPN TLLKSYKRIT NNRCTLKAIV FKTKLGKEICADPKKKWVQD ATKHLDQKLQ TPKP.
What applications can EOTAXIN RAT Protein be used in?
EOTAXIN RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EOTAXIN RAT Protein?
The endotoxin level is minimal, EOTAXIN RAT 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 :
SEMA7A HumanDescription:
Semaphorin 7A Human Recombinant
Semaphorin-7A, CDw108, JMH blood group antigen, John-Milton-Hargen human blood group Ag, Semaphorin-K1, Sema K1, Semaphorin-L, Sema L, CD108.
Product # :
PRO-2506Price :
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Shipped with Ice Packs
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Description
SEMA7A produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 846 amino acids (45-648 a.a.) and having a molecular mass of 95.7kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).SEMA7A is expressed with an 242 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
SEMA7A protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
SEMA7A (semaphorin-7A isoform 1), is a membrane-bound semaphorin which is linked with cell surfaces via a glycosylphosphatidylinositol (GPI) linkage. SEMA7A encourages formation of focal adhesion complexes, activation of the protein kinase PTK2/FAK1 and subsequent phosphorylation of MAPK3 & MAPK1. SEMA7A takes a vital part in integrin-mediated signaling and functions in regulating cell migration as well as immune responses. In addition, SEMA7A promotes the production of proinflammatory cytokines by macrophages & monocytes.
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Synonyms
Semaphorin-7A, CDw108, JMH blood group antigen, John-Milton-Hargen human blood group Ag, Semaphorin-K1, Sema K1, Semaphorin-L, Sema L, CD108.
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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
ADPQGHLRSG PRIFAVWKGH VGQDRVDFGQ TEPHTVLFHE PGSSSVWVGG RGKVYLFDFP EGKNASVRTV NIGSTKGSCL DKRDCENYIT LLERRSEGLL ACGTNARHPS CWNLVNGTVV PLGEMRGYAP FSPDENSLVL FEGDEVYSTI RKQEYNGKIP RFRRIRGESE LYTSDTVMQN PQFIKATIVH QDQAYDDKIY YFFREDNPDK NPEAPLNVSR VAQLCRGDQG GESSLSVSKW NTFLKAMLVC SDAATNKNFN RLQDVFLLPD PSGQWRDTRV YGVFSNPWNY SAVCVYSLGD IDKVFRTSSL KGYHSSLPNP RPGKCLPDQQ PIPTETFQVA DRHPEVAQRV EPMGPLKTPL FHSKYHYQKV AVHRMQASHG ETFHVLYLTT DRGTIHKVVE PGEQEHSFAF NIMEIQPFRR AAAIQTMSLD AERRKLYVSS QWEVSQVPLD LCEVYGGGCH GCLMSRDPYC GWDQGRCISI YSSERSVLQS INPAEPHKEC PNPKPDKAPL QKVSLAPNSR YYLSCPMESR HATYSWRHKE NVEQSCEPGH QSPNCILFIE NLTAQQYGHY FCEAQEGSYF REAQHWQLLP EDGIMAEHLL GHACALALEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH.
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 :
SERPINA9 MouseDescription:
Serpin Peptidase Inhibitor, Clade A Mouse Recombinant
Serpin A9, Serpina9, SERPINA9.
Product # :
PRO-2366Price :
Quantity :
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Description
SERPINA9 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 401 amino acids (26-418 a.a) and having a molecular mass of 45.2kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).SERPINA9 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
SERPINA9 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Serpin Peptidase Inhibitor, Clade A Member 9, also known as serpin A9, belongs to the Serpin superfamily of serine protease inhibitors. Serpins are the most extensively distributed superfamily of protease inhibitors which use a conformational modification to inhibit target enzymes. Serpins are known to inhibit serine proteases as well as inhibiting caspases in addition to papain-like cysteine proteases. Serpins are conformational labile and numerous of the disease-linked mutations of serpins outcome in misfolding or in pathogenic, inactive polymers. serpin A9 demonstrates inhibition towards trypsin, thrombin, as well as plasmin and binds DNA and heparin.
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Synonyms
Serpin A9, Serpina9, SERPINA9.
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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
NPYNQESSHL PSMKKNPASQ VSPSNTRFSF LLYQRLAQEN PGQNILFSPV SISTSLAMLS LGARSATKTQ ILRTLGFNFT WVSEPTIHMG FEYLVRSLNK CHQGRELRMG SVLFIRKELQ LQATFLDRVK KLYGAKVFSE DFSNAATAQA QINSYVEKET KGKVVDVIQD LDSQTAMVLV NHIFFKANWT QPFSTANTNK SFPFLLSKGT TVHVPMMHQT ESFAFGVDKE LGCSILQMDY RGDAVAFFVL PGKGKMRQLE KSLSARRLRK WSRSLQKRWI KVFIPKFSIS ASYNLETILP KMGIRDAFNS NADFSGITKT HFLQVSKAAH KAVLDVSEEG TEAAAATTTK LIVRSRDTPS SIIAFKEPFL ILLLDKNTES VLFLGKVENP RKMLEHHHHH H
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 :
OstreolysinDescription:
Ostreolysin Pleurotus Ostreatus Recombinant
Product # :
PRO-2600Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Pleurotus Ostreatus Ostreolysin Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 137 amino acids and having a molecular mass of 15 kDa. The Ostreolysin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Ostreolysin protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Ostreolysin has potent anti-carcinogenic activity in several colon cancer cell lines.
More Info
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Introduction
Ostreolysin is extracted from Pleurotus ostreatus (oyster mushroom). It is a pore forming protein, which contains a lytic part to both cholesterol and sphingomyelin containing membranes. Because of their cholesterol content and the appearance of ostreolysin in the detergent resistant membranes, ostreolysin is cytotoxic towards the ovary cells of Chinese hamster. It seems that Ostreolysin spots a rich lipid cholesterol phase, presumably the liquid ordered phase.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Pleurotus Ostreatus Ostreolysin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon C between 2-7 days and for future use reconstituted Ostreolysin should be stored at 4°C below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please avoid freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Ostreolysin in sterile 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The N-terminal amino sequence is Ala-Tyr-Ala-Gln-Trp-Val.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 2.64 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNA-man computer analysis program.
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 :
ESM1 Human, SF9Description:
Endothelial Cell-Specific Molecule 1 Human Recombinant, Sf9
Endothelial Cell Specific Molecule 1, Endothelial Cell-Specific Molecule 1, ESM-1, Endocan.
Product # :
PRO-2588Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ESM1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 174 amino acids (20-184a.a.) and having a molecular mass of 19.2kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). ESM1 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ESM1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
ESM1, also knows as, Endothelial cell-specific molecule 1 is a protein encoded by a gene called ESM1 in humans. ESM1 is a secreted protein that is highly expressed in human kidney and lung tissues (in the endothelial cells). There are suggestions regarding the protein’s involvement in endothelium-dependent pathological diseases, due to his regulation that is performed by cytokines.
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Synonyms
Endothelial Cell Specific Molecule 1, Endothelial Cell-Specific Molecule 1, ESM-1, Endocan.
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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
ADLWSNNYAV DCPQHCDSSE CKSSPRCKRT VLDDCGCCRV CAAGRGETCY RTVSGMDGMK CGPGLRCQPS NGEDPFGEEF GICKDCPYGT FGMDCRETCN CQSGICDRGT GKCLKFPFFQ YSVTKSSNRF VSLTEHDMAS GDGNIVREEV VKENAAGSPV MRKWLNPRHH 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 :
FGF 2 RatDescription:
Fibroblast Growth Factor-basic Rat Recombinant
HBGH-2, HBGF-2, Prostatropin, FGF-2, FGB-b, Fibroblast Growth Factor-basic, Basic fibroblast growth factor, bFGF, Heparin-binding growth factor 2.
Product # :
CYT-608Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
bFGF Rat Recombinant (FGF-2) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16.4 kDa.The bFGF2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FGF-b was lyophilized from 1mg/ml solution after extensive dialysis against 10mM Na2PO4, pH 7.5 and 50mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 range as determined by the dose-dependant proliferation of NR6R-3T3 cells was found to be 0.903ng/ml, corresponding to a specific activity of 1.1x107 units/mg.
More Info
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Introduction
FGF-basic is a member of the fibroblast growth factor (FGF) family. FGF family members bind heparin and possess broad mitogenic and angiogenic activities. This protein has been implicated in diverse biological processes, such as limb and nervous system development, wound healing, and tumor growth. The mRNA for this gene contains multiple polyadenylation sites, and is alternatively translated from AUG and non-AUG (CUG) initiation codons resulting in five different isoforms with distinct properties. The CUG-initiated isoforms are localized in the nucleus and are responsible for the intracrine effect, whereas, the AUG-initiated form is mostly cytosolic and is responsible for the paracrine and autocrine effects of this FGF.
The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. there are differences in the tissue distribution and concentration of these 2 growth factors. -
Synonyms
HBGH-2, HBGF-2, Prostatropin, FGF-2, FGB-b, Fibroblast Growth Factor-basic, Basic fibroblast growth factor, bFGF, Heparin-binding growth factor 2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Rat bFGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Rat FGF-2 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 Rat bFGF 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
MPALPEDGGGA FPPGHFKDPK RLYCKNGGFF LRIHPDGRVD GVREKSDPHV KLQLQAEERG VVSIKGVCAN RYLAMKEDGR LLASKCVTEE CFFFERLESN NYNTYRSRKY SSWYVALKRT GQYKLGSKTG PGQKAILFLP MSAKS.
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Background
What is the molecular weight/Mw of FGF 2 RAT Protein?
FGF 2 RAT Protein has a total Mw of 16.4kDa.
What is the source or expression system of FGF 2 RAT Protein?
Escherichia Coli.
What is the Purity of FGF 2 RAT Protein?
FGF 2 RAT Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF 2 RAT Protein?
The ED50 range as determined by the dose-dependant proliferation of NR6R-3T3 cells was found to be 0.903ng/ml, corresponding to a specific activity of 1.1x107 units/mg.
What is the amino acid sequence of FGF 2 RAT Protein?
MPALPEDGGGA FPPGHFKDPK RLYCKNGGFF LRIHPDGRVD GVREKSDPHV KLQLQAEERG VVSIKGVCAN RYLAMKEDGR LLASKCVTEE CFFFERLESN NYNTYRSRKY SSWYVALKRT GQYKLGSKTG PGQKAILFLP MSAKS.
What applications can FGF 2 RAT Protein be used in?
FGF 2 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF 2 RAT Protein?
The endotoxin level is minimal, FGF 2 RAT 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 :
JAM3 HumanDescription:
Junctional Adhesion Molecule 3 Human Recombinant
Junctional Adhesion Molecule 3, Junctional Adhesion Molecule C, JAM-C, JAM-2, JAM-3.
Product # :
PRO-1223Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
JAM3 Human Recombinant produced in E. coli is a single polypeptide chain containing 234 amino acids (32-241) and having a molecular mass of 26.0 kDa.JAM3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The JAM3 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM EDTA, 5mM DTT and 50% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
JAM3 belongs to the junctional adhesion molecule protein family and functions as a receptor for another member of this family. JAM3 plays a part in cell-cell adhesion. The soluble form of JAM3 is a mediator of angiogenesis. JAM3 is a counter-receptor for ITGAM, mediating leukocyte-platelet interactions and is involved in the regulation of transepithelial migration of polymorphonuclear neutrophils (PMN). A mutation in an intron of the JAM3 gene is linked with hemorrhagic destruction of the brain, subependymal calcification, and congenital cataracts.
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Synonyms
Junctional Adhesion Molecule 3, Junctional Adhesion Molecule C, JAM-C, JAM-2, JAM-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 MGSMVNLKSS NRTPVVQEFE SVELSCIITD SQTSDPRIEW KKIQDEQTTY VFFDNKIQGD LAGRAEILGK TSLKIWNVTR RDSALYRCEV VARNDRKEID EIVIELTVQV KPVTPVCRVP KAVPVGKMAT LHCQESEGHP RPHYSWYRND VPLPTDSRAN PRFRNSSFHL NSETGTLVFT AVHKDDSGQY YCIASNDAGS ARCEEQEMEV YDLN
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 :
CDH5 MouseDescription:
Cadherin 5 Mouse Recombinant
Cadherin-5, Vascular endothelial cadherin, VE-cadherin, CD144, Cdh5.
Product # :
PRO-2244Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CDH5 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 583 amino acids (25-599a.a.) and having a molecular mass of 66.2kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).CDH5 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
CDH5 protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Cadherin-5, also known as CDH5 is a classical cadherin which belongs to the cadherin superfamily. The CDH5is located in a six-cadherin cluster in a region on the long arm of chromosome 16 which is involved in loss ofheterozygosity events in breast as well as prostate cancer. CDH5 is a calcium-dependent cell-celladhesion glycoprotein composed of five extracellular cadherin repeats, a transmembrane region and a highlyconserved cytoplasmic tail. Furthermore, CDH5 functions as a classic cadherin by passing on to cells the ability to adhere in ahomophilic manner, CDH5 plays a significant role in endothelial cell biology through control of the cohesion as well as organization of the intercellular junctions.
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Synonyms
Cadherin-5, Vascular endothelial cadherin, VE-cadherin, CD144, Cdh5.
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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
GPNFPQIDTP NMLPAHHRQK RDWIWNQMHI DEEKNESLPH YVGKIKSNVN RQNAKYVLQG EFAGKIFGVD ANTGNVLAYE RLDREKVSEY FLTALIVDKN TNKNLEQPSS FTVKVHDIND NWPVFSHQVF NASVPEMSAI GTSVIRVTAV DADDPTVAGH ATVLYQIVKG NEYFSIDNSG LIFTKIKNLD REKQAEYKIV VETQDALGLR GESGTATVMI RLEDINDNFP VFTQSTYTFS VPEDIRVGKP LGFLTVVDPD EPQNRMTKYS IMQGEYRDTF TIETDPKRNE GIIKPTKSLD YEVIQQYTFY IEATDPTIRY EYLSSTSGKN KAMVTINVLD VDEPPVFQRH FYHFKLPENQ KKPLIGTVVA KDPDKAQRSI GYSIRKTSDR GQFFRITKQG NIYNEKELDR ETYAWYNLTV EANELDSRGN PVGKESIVQV YIEVLDENDN PPEFAQPYEP KVCENAAQGK LVVQISATDK DVVPVNPKFK FALKNEDSNF TLINNHDNTA NITVKYGQFN REHAKFHYLP VLISDNGVPS LTGTSTLTVG VCKCNEQGEF TFCEEMAAQA GVSIQLEHHH HHH.
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 :
SPA, HisDescription:
Staphylococcal Protein-A Recombinant, His Tag
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
Product # :
PRO-1925Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
SPA Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain fused with 6×His tag at C-terminus. SPA is comprised of 5 IgG-binding domains E-D-A-B-C aligned in series containing 306 amino acids and having a molecular mass of 34.7kDa containing little or no carbohydrate. Cell wall binding region, cell membrane binding region and albumin binding region were removed to ensure the highest specific IgG binding.
Source
Escherichia Coli.
Formulation
SPA protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by:
(a) Analysis by HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Protein A is a cell wall component produced by several strains of Staphylococcus aureus. The recombinant Protein A is genetically engineered protein and holds 5 IgG-binding regions of protein A. Recombinant Protein A functions basically the same as native Protein A and is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein A binds to human IgG1, IgG2 and IgG4, mouse IgG2a, IgG2b and IgG3 and rat IgG2c. Protein A also binds to total IgG from rabbit, pig, dog, cat, and guinea pig.
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Synonyms
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SPA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SPA 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 SPA in sterile 18MΩ-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MNAAQHDEAQ QNAFYQVLNM PNLNADQRNG FIQSLKDDPS QSANVLGEAQ KLNDSQAPKA DAQQNNFNKD QQSAFYEILN MPNLNEAQRN GFIQSLKDDP SQSTNVLGEA KKLNESQAPK ADNNFNKEQQ NAFYEILNMP NLNEEQRNGF IQSLKDDPSQ SANLLSEAKK LNESQAPKAD NKFNKEQQNA FYEILHLPNL NEEQRNGFIQ SLKDDPSQSA NLLAEAKKLN DAQAPKADNK FNKEQQNAFY EILHLPNLTE EQRNGFIQSL KDDPSVSKEI LAEAKKLNDA QAPKEEDSLE HHHHHH.
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 :
TNIP1 HumanDescription:
TNFAIP3 Interacting Protein 1 Human Recombinant
TNFAIP3-interacting protein 1, HIV-1 Nef-interacting protein, Nef-associated factor 1, Naf1, Nip40-1, Virion-associated nuclear shuttling protein, VAN, hVAN, TNIP1, KIAA0113, NAF1, ABIN-1.
Product # :
PRO-005Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TNIP1 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 458 amino acids (94-530 a.a.) and having a molecular mass of 51.8kDa. The TNIP1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TNIP1 solution (0.25 mg/ml) contains 20mM Tris-HCl buffer (pH7.5), 20% glycerol, 5mM DTT and 200mM NaCl.
Purity
Greater than 75.0% as determined by SDS-PAGE.
More Info
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Introduction
TNFAIP3-interacting protein 1 (TNIP1) interacts with zinc finger protein A20/TNFAIP3 and inhibits TNF-induced NF-kappa-B-dependent gene expression by interfering with a RIP- or TRAF2-mediated transactivation signal. Furthermore, TNIP1 interacts with HIV-1 matrix protein and is packaged into virions and its overexpression can inhibit viral replication. TNIP1 can regulate matrix nuclear localization, both nuclear import of Preintegration complex (PIC) and export of GAG polyprotein and viral genomic RNA during virion production.
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Synonyms
TNFAIP3-interacting protein 1, HIV-1 Nef-interacting protein, Nef-associated factor 1, Naf1, Nip40-1, Virion-associated nuclear shuttling protein, VAN, hVAN, TNIP1, KIAA0113, NAF1, ABIN-1.
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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 MSNVTASPTA PACPSDKPAP VQKPPSSGTS SEFEVVTPEE QNSPESSSHA NAMALGPLPR EDGNLMLHLQ RLETTLSVCA EEPDHGQLFT HLGRMALEFN RLASKVHKNE QRTSILQTLC EQLRKENEAL KAKLDKGLEQ RDQAAERLRE ENLELKKLLM SNGNKEGASG RPGSPKMEGT GKKAVAGQQQ ASVTAGKVPE VVALGAAEKK VKMLEQQRSE LLEVNKQWDQ HFRSMKQQYE QKITELRQKL ADLQKQVTDL EAEREQKQRD FDRKLLLAKS KIEMEETDKE QLTAEAKELR QKVKYLQDQL SPLTRQREYQ EKEIQRLNKA LEEALSIQTP PSSPPTAFGS PEGAGALLRK QELVTQNELL KQQVKIFEED FQRERSDRER MNEEKEELKK QVEKLQAQVT LSNAQLKAFK DEEKAREALR QQKRKAKA.
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 :
PSMB10 HumanDescription:
Proteasome Beta Type 10 Human Recombinant
Proteasome subunit beta type-10, Low molecular mass protein 10, Macropain subunit MECl-1, Multicatalytic endopeptidase complex subunit MECl-1, Proteasome MECl-1, Proteasome subunit beta-2i, PSMB10, LMP10, MECL1, beta2i, MGC1665, FLJ00366.
Product # :
PRO-931Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PSMB10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 255 amino acids (40-273 a.a.) and having a molecular mass of 26.9kDa.PSMB10 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PSMB10 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
PSMB10 is a member of the proteasome B-type family (T1B family) which is a 20S core beta subunit. The proteasome is a multicatalytic proteinase complex with an extremely ordered ring-shaped 20S core structure. This core structure is comprised of four rings of 28 non-identical subunits; two rings are composed of seven alpha subunits and two rings are composed of seven beta subunits. Proteasomes are circulated in eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. A crucial function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. PSMB10 gene expression is induced by INFg, and it replaces catalytic subunit 2 (proteasome beta 7 subunit) in the immunoproteasome.
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Synonyms
Proteasome subunit beta type-10, Low molecular mass protein 10, Macropain subunit MECl-1, Multicatalytic endopeptidase complex subunit MECl-1, Proteasome MECl-1, Proteasome subunit beta-2i, PSMB10, LMP10, MECL1, beta2i, MGC1665, FLJ00366.
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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 MTTIAGLVFQ DGVILGADTR ATNDSVVADK SCEKIHFIAP KIYCCGAGVA ADAEMTTRMV ASKMELHALS TGREPRVATV TRILRQTLFR YQGHVGASLI VGGVDLTGPQ LYGVHPHGSY SRLPFTALGS GQDAALAVLE DRFQPNMTLE AAQGLLVEAV
TAGILGDLGS GGNVDACVIT KTGAKLLRTL SSPTEPVKRS GRYHFVPGTT AVLTQTVKPL TLELVEETVQ AMEVE.
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
More Info
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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.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 :
BMP4 Human, CHODescription:
Bone Morphogenetic protein-4 Active Human Recombinant, CHO
BMP4, ZYME, BMP2B, BMP2B1.
Product # :
CYT-1093Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Bone Morphogenetic protein-4 Active Human Recombinant produced in CHO cells is a glycosylated homodimer chain containing 2x116 amino acids and having a total molecular mass of 26.2kDa. BMP4 is purified by proprietary chromatographic techniques.
Source
CHO cells.
Formulation
The protein was lyophilized from a sterile (0.2µm) filtered solution containing 0.1% Trifluoroacetic Acid (TFA).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as calculated by Alkaline phosphatase activity induced in ATDC-5 cells is 15ng/ml corresponding to a specific activity which is 6.7 x 10^4 units/mg.
More Info
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Introduction
The protein encoded by this gene is a member of the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily.
The superfamily includes large families of growth and differentiation factors.
Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site.
This particular family member plays an important role in the onset of endochondral bone formation in humans, and a reduction in expression has been associated with a variety of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva.
Alternative splicing in the 5' untranslated region of this gene has been described and three variants are described, all encoding an identical protein.
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Synonyms
BMP4, ZYME, BMP2B, BMP2B1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BMP4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP4 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 BMP4 in sterile 10mM HCl at a concentration of 0.1 mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAI VQT LVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.
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Background
What is the molecular weight/Mw of BMP4 Protein?
BMP4 Protein has a total Mw of 26.4kDa.
What is the source or expression system of BMP4 Protein?
CHO cells.
What is the Purity of BMP4 Protein?
BMP4 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BMP4 Protein?
The ED50, as calculated by Alkaline phosphatase activity induced in ATDC-5 cells is 15ng/ml corresponding to a specific activity which is 6.7 x 10^4 units/mg.
What is the amino acid sequence of BMP4 Protein?
SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAI VQT LVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.
What applications can BMP4 Protein be used in?
BMP4 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BMP4 Protein?
The endotoxin level is minimal, BMP4 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 :
L1CAM HumanDescription:
L1 Cell Adhesion Molecule Human Recombinant
L1 Cell Adhesion Molecule, Antigen Identified By Monoclonal Antibody R1, N-CAM-L1, NCAM-L1, CAML1, MIC5, Neural Cell Adhesion Molecule L1, CD171 Antigen, N-CAML1, CD171, HSAS1, MASA, HSAS, SPG1, S10.
Product # :
PRO-2446Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
L1CAM Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 1104 amino acids (20-1115a.a.) and having a molecular mass of 123.6kDa (Molecular size on SDS-PAGE will appear at approximately 100-150kDa). L1CAM is expressed with a 8 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
L1CAM protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
More to 30% measured by the ability of the immobilized protein to support the adhesion of Neuro-2a mouse neuroblastoma cells. When cells are added to human L1CAM coated plates 1 ug/ml.
More Info
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Introduction
L1 Cell Adhesion Molecule (L1CAM) which is a cell adhesion receptor of the immunoglobulin superfamily takes part in nerve cell function. L1CAM is a neural cell adhesion molecule involved in the dynamics of cell adhesion and in the generation of transmembrane signals at tyrosine kinase receptors. L1CAM takes part in cell migration, neurite outgrowth and myelination. Furthermore, L1CAM plays an important role in the dynamics of neuronal structure and function in the mature brain.
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Synonyms
L1 Cell Adhesion Molecule, Antigen Identified By Monoclonal Antibody R1, N-CAM-L1, NCAM-L1, CAML1, MIC5, Neural Cell Adhesion Molecule L1, CD171 Antigen, N-CAML1, CD171, HSAS1, MASA, HSAS, SPG1, S10.
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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
IQIPEELMEP PVITEQSPRR LVVFPTDDIS LKCEASGKPE VQFRWTRDGV HFKPKEELGV TVYQSPHSGS FTITGNNSNF AQRFQGIYRC FASNKLGTAM SHEIRLMAEG APKWPKETVK PVEVEEGESV VLPCNPPPSA EPLRIYWMNS KILHIKQDER VTMGQNGNLY FANVLTSDNH SDYICHAHFP GTRTIIQKEP IDLRVKATNS MIDRKPRLLF PTNSSSHLVA LQGQPLVLEC IAEGFPTPTI KWLRPSGPMP ADRVTYQNHN KTLQLLKVGE EDDGEYRCLA ENSLGSARHA YYVTVEAAPY WLHKPQSHLY GPGETARLDC QVQGRPQPEV TWRINGIPVE ELAKDQKYRI QRGALILSNV QPSDTMVTQC EARNRHGLLL ANAYIYVVQL PAKILTADNQ TYMAVQGSTA YLLCKAFGAP VPSVQWLDED GTTVLQDERF FPYANGTLGI RDLQANDTGR YFCLAANDQN NVTIMANLKV KDATQITQGP RSTIEKKGSR VTFTCQASFD PSLQPSITWR GDGRDLQELG DSDKYFIEDG RLVIHSLDYS DQGNYSCVAS TELDVVESRA QLLVVGSPGP VPRLVLSDLH LLTQSQVRVS WSPAEDHNAP IEKYDIEFED KEMAPEKWYS LGKVPGNQTS TTLKLSPYVH YTFRVTAINK YGPGEPSPVS ETVVTPEAAP EKNPVDVKGE GNETTNMVIT WKPLRWMDWN APQVQYRVQW RPQGTRGPWQ EQIVSDPFLV VSNTSTFVPY EIKVQAVNSQ GKGPEPQVTI GYSGEDYPQA IPELEGIEIL NSSAVLVKWR PVDLAQVKGH LRGYNVTYWR EGSQRKHSKR HIHKDHVVVP ANTTSVILSG LRPYSSYHLE VQAFNGRGSG PASEFTFSTP EGVPGHPEAL HLECQSNTSL LLRWQPPLSH NGVLTGYVLS YHPLDEGGKG QLSFNLRDPE LRTHNLTDLS PHLRYRFQLQ ATTKEGPGEA IVREGGTMAL SGISDFGNIS ATAGENYSVV SWVPKEGQCN FRFHILFKAL GEEKGGASLS PQYVSYNQSS YTQWDLQPDT DYEIHLFKER MFRHQMAVKT NGTGRVRLPP AGFATELEHH 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 :
CoV-2-S1 (319-541), BiotinDescription:
Coronavirus 2019 Spike Glycoprotein-S1 Receptor Binding Domain (319-541 a.a), Biotinylated Recombinant
Product # :
SARS-030Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
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Description
The HEK293 derived Biotinylated recombinant protein contains the Coronavirus 2019 Spike Glycoprotein S1 Receptor Binding Domain [ RBD ], Wuhan-Hu-1 strain, amino acids 319-541 fused to His tag & AVI tag at C-terminal and having a molecular mass of 28.7kDa.
Source
HEK293 Cells.
Formulation
CoV-2 S1 RBD protein is lyophilized from 1x PBS pH-7.4 + 10% trehalose.
Purity
Protein is >90% pure as determined SDS-PAGE.
More Info
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Introduction
A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.
The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.
While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.
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Physical Appearance
Lyophilized freezed dried powder.
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Stability
Lyophilized Cov-2 S1 Glycoprotein RBD although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CoV2 Spike protein 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 CoV-2 S1 protein in sterile 18M-cm H2O at aconcentration of 0.2mg/ml and not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Purification Method
Purified by Metal-Afinity chromatographic technique.
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 :
p59-Fyn HumanDescription:
p59-Fyn Human Recombinant
Proto-oncogene tyrosine-protein kinase Fyn, EC 2.7.10.2, p59-Fyn, Protooncogene Syn, SLK, FYN, MGC45350, Fyn p59.
Product # :
PRO-506Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
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Description
p59-Fyn Human Recombinant (a.a. 23-216) expressed in E.coli, shows a 50 kDa SDS-PAGE (Including GST tag).The p59-Fyn is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
p59-Fyn in 50mM Tris-Acetate, pH7.5, 1mM EDTA and 20% Glycerol.
More Info
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Introduction
p59-Fyn is a member of the protein-tyrosine kinase oncogene family. p59fyn is a membrane-associated non-receptor protein tyrosine kinase that belongs to the Src-family of kinases. p59-Fyn encodes a membrane-associated tyrosine kinase which is implicated in the control of cell growth. p59-Fyn associates with the p85 subunit of phosphatidylinositol 3-kinase and interacts with the fyn-binding protein. The unique N-terminal domain of p59fyn interacts with the CD3 and eta chains of the TcR. p59fyn can bind other proteins (p82 and p116) through its SH2 and SH3 domains, which may act as substrates or regulators of fyn activity. p59fyn is highly expressed in brain suggesting that it may have a role in the sensory nervous network and in myelination at early stages of CNS formation. Distinct isoforms exist due to alternative splicing.
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Synonyms
Proto-oncogene tyrosine-protein kinase Fyn, EC 2.7.10.2, p59-Fyn, Protooncogene Syn, SLK, FYN, MGC45350, Fyn p59.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months.Please prevent freeze-thaw cycles.
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Applications
• ELISA
• Inhibition Assays
• Western Blotting.
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 :
BuserelinDescription:
Buserelin
Product # :
HOR-255Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Buserelin contains 9 amino acids Glu-His-Trp-Ser-Tyr-D-Ser(tBu)-Leu-Arg-Pro-NHEt and having a molecular weight of 1239.44 Dalton.
Formulation
The Buserelin peptide was lyophilized with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Buserelin belongs to the group of gonadotrophin releasing hormone (gonadorelin) analogues (LHRH agonist). It acts on the pituitary gland which controls the amount of many different types of hormones (chemical messengers). It alters the amount of hormones, particularly the oestrogens androgens. This alteration of hormone levels can be exploited to treat cancers of the prostate gland, which are stimulated to grow by testosterone. Buserelin lowers the levels of testosterone, which starves the tumour of testosterone and causes it to shrink.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Buserelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Buserelin 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 Buserelin in sterile 18MΩ-cm H2O not less than 100 µg/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 :
Leptin qA Rat, PEGDescription:
Leptin Quadruple Antagonist, Pegylated Rat Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-1241Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- formulation
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Description
Leptin Pegylated Quadruple Antagonist Rat Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids. The Rat Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Rat Leptin Pegylated Quadruple Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Rat Leptin Pegylated Quadruple Antagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Rat Leptin Pegylated Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro.
More Info
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Rat Leptin Pegylated Quadruple Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 and up to 2mM of rat pegylated leptin antagonist and filter sterilization rat pegylated leptin antagonist can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Rat Leptin Pegylated Quadruple Antagonist in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Background
Leptin is a hormone which mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin receptors are expressed by various brain and peripheral cell types. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings. High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
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 :
Leptin tA RatDescription:
Leptin Antagonist Triple Mutant Rat Recombinant
Product # :
CYT-355Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
- formulation
- purity
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Description
Leptin Antagonist Triple Mutant Rat Recombinant is a singly non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A mutant. Leptin Antagonist Triple Mutant Rat Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (0.85mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
ProSpec’s Leptin Antagonist Triple Mutant Rat Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin-Antagonist Triple Mutant Rat Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2 mM and filter sterilization LEP-tA mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Rat Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.
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Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.21 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
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.