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1000 results found for “Chagas”
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Name :
HMGCL HumanDescription:
3-Hydroxymethyl-3-Methylglutaryl-CoA Lyase Human Recombinant
Hydroxymethylglutaryl-CoA lyase mitochondrial, HL, HMG-CoA lyase, 3-hydroxy-3-methylglutarate-CoA lyase, HMGCL.
Product # :
ENZ-218Price :
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Description
HMGCL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (28-325) and having a molecular mass of 34.2kDa.HMGCL is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HMGCL solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Hydroxymethylglutaryl-CoA lyase (HMGCL) is a mitochondrial matrix protein which is a member of the HMG-CoA lyase family. HMGCL is a homodimer and participates in leucine catabolism and ketogenesis, the hepatic synthesis of ketone bodies which, during fasting, provides a major source of energy for the heart, brain and kidney. More precisely, HMGCL catalyzes the final step of these processes, the cleavage of 3-hydroxy-3-methylglutaryl-CoA to acetoacetic acid and acetyl-CoA.
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Synonyms
Hydroxymethylglutaryl-CoA lyase mitochondrial, HL, HMG-CoA lyase, 3-hydroxy-3-methylglutarate-CoA lyase, HMGCL.
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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 MGSHMTLPKR VKIVEVGPRD GLQNEKNIVS TPVKIKLIDM LSEAGLSVIE TTSFVSPKWV PQMGDHTEVL KGIQKFPGIN YPVLTPNLKG FEAAVAAGAK EVVIFGAASE LFTKKNINCS IEESFQRFDA ILKAAQSANI SVRGYVSCAL GCPYEGKISP AKVAEVTKKF YSMGCYEISL GDTIGVGTPG IMKDMLSAVM QEVPLAALAV HCHDTYGQAL ANTLMALQMG VSVVDSSVAG LGGCPYAQGA SGNLATEDLV YMLEGLGIHT GVNLQKLLEA GNFICQALNR KTSSKVAQAT CKL.
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 :
ANSA E.coliDescription:
Cytoplasmic L-asparaginase I E.Coli Recombinant
L-asparaginase 1, L-asparaginase I, L-ASNase I, L-asparagine amidohydrolase I, ansA, b1767, JW1756.
Product # :
ENZ-119Price :
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Description
ANSA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 358 amino acids (1-338 a.a.) and having a molecular mass of 39.3kDa.ANSA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ANSA solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 2mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
AnsA is a cytoplasmic asparaginase from E.coli involved in intracellular asparagine utilization. E.coli has 2 L-asparaginases: the cytoplasmic type I form (ansA) and the periplasmic type II form (ansB). AnsA (Type L asparaginase) is constitutively expressed and is obligatory for the growth of the bacteria on asparagine as the sole nitrogen source.
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Synonyms
L-asparaginase 1, L-asparaginase I, L-ASNase I, L-asparagine amidohydrolase I, ansA, b1767, JW1756.
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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 MQKKSIYVAY TGGTIGMQRS EQGYIPVSGH LQRQLALMPE FHRPEMPDFT IHEYTPLMDS SDMTPEDWQH IAEDIKAHYD DYDGFVILHG TDTMAYTASA LSFMLENLGK PVIVTGSQIP LAELRSDGQI NLLNALYVAA NYPINEVTLF FNNRLYRGNR TTKAHADGFD AFASPNLPPL LEAGIHIRRL NTPPAPHGEG ELIVHPITPQ PIGVVTIYPG ISADVVRNFL RQPVKALILR SYGVGNAPQN KAFLQELQEA SDRGIVVVNL TQCMSGKVNM GGYATGNALA HAGVIGGADM TVEATLTKLH YLLSQELDTE TIRKAMSQNL RGELTPDD.
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 :
NDRG1 HumanDescription:
N-Myc Downstream Regulated 1 Human Recombinant
Protein NDRG1, N-myc downstream-regulated gene 1 protein, Differentiation-related gene 1 protein, Reducing agents and tunicamycin-responsive protein, Nickel-specific induction protein Cap43, DRG-1, RTP, Rit42, NDRG1, CAP43, DRG1, GC4, NDR1, NMSL, TDD5, CMT4D, HMSNL, TARG1, PROXY1.
Product # :
PRO-724Price :
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Description
NDRG1 Human Recombinant fused with 8 amino acid His tag at C-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 402 amino acids (1-394 a.a.) and having a molecular mass of 43.9 kDa.The NDRG1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NDRG1 solution contains 20mM Tris-HCl buffer (pH8.0), 0.1mM PMSF and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using MCF7 cell. The ED50 for this effect is 0.5 - 1.5ng/ml, corresponding to a Specific Activity of 666,000 -2,000,000 IU/mg.Citations
More Info
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Introduction
NDRG1 is a cytoplasmic protein that is involved in stress responses, hormone responses, cell growth, and differentiation. NDRG1 is one of 4 members of the NDRG ?/?-hydrolase family. NDRG1 is classified in databases as a tumor suppressor and heavy metal-response protein. NDRG1’s functions include cell-cycle regulation, cellular differentiation, apoptosis, hypoxia response and metal-ion sensing. NDRG1 is also essential for p53-mediated caspase activation and apoptosis. The NDRG1 is a Rab4a effector that is involved in vesicular recycling of E-cadherin. NDRG1 is ubiquitous; it is expressed most notably in placental membranes and prostate, kidney, small intestine, and ovary tissues. NDRG1 has reduced expression in adenocarcinomas compared to normal tissues.
NDRG1 gene mutations are reported to be the cause for hereditary motor and sensory neuropathy-Lom (HMSNL), which is a severe autosomal recessive form of Charcot- Marie-Tooth (CMT) disease. In addition, decreased NDRG1 expression in glioma is linked to tumor progression. On the other hand, overexpression of NDRG1 is connected to malignant status of esophageal cancer. NDRG1 may also have a role in portal vein invasion and intrahepatic metastasis in human hepatocellular carcinoma. -
Synonyms
Protein NDRG1, N-myc downstream-regulated gene 1 protein, Differentiation-related gene 1 protein, Reducing agents and tunicamycin-responsive protein, Nickel-specific induction protein Cap43, DRG-1, RTP, Rit42, NDRG1, CAP43, DRG1, GC4, NDR1, NMSL, TDD5, CMT4D, HMSNL, TARG1, PROXY1.
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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
MSREMQDVDL AEVKPLVEKG ETITGLLQEF DVQEQDIETL HGSVHVTLCG TPKGNRPVIL TYHDIGMNHK TCYNPLFNYE DMQEITQHFA
VCHVDAPGQQ DGAASFPAGY MYPSMDQLAE MLPGVLQQFG LKSIIGMGTG AGAYILTRFA LNNPEMVEGL VLINVNPCAE GWMDWAASKI SGWTQALPDM VVSHLFGKEE MQSNVEVVHT YRQHIVNDMN PGNLHLFINA YNSRRDLEIE RPMPGTHTVT LQCPALLVVG DSSPAVDAVV ECNSKLDPTK TTLLKMADCG GLPQISQPAK LAEAFKYFVQ GMGYMPSASM TRLMRSRTAS GSSVTSLDGT RSRSHTSEGT RSRSHTSEGT RSRSHTSEGA HLDITPNSGA AGNSAGPKSM EVSCLEHHHH HH
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 :
CXCL11 HumanDescription:
I-TAC Human Recombinant (CXCL11)
Small inducible cytokine B11, CXCL11, I-TAC, IP-9, H174, Beta-R1, chemokine (C-X-C motif) ligand 11, IP9, b-R1, SCYB11, SCYB9B, MGC102770.
Product # :
CHM-334Price :
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Shipped at Room temp
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Description
I-TAC Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 8300 Dalton. The I-TAC is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2?m filtered concentrated (0.5mg/ml) solution in 20mM PB, pH 7.4, 100mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human IL-2 activated T-Lymphocytes using a concentration range of 0.1-10.0 ng/ml.Citations
More Info
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Introduction
Chemokine (C-X-C motif) ligand 11 (CXCL11) is a small cytokine belonging to the CXC chemokinen family that is also called inducible T-cell alpha chemoattractant (I-TAC) and (IP-9). I-TAC is highly expressed in peripheral blood leukocytes, pancreas and liver, with moderate levels in thymus, spleen and lung and low expression levels were in small intestine, placenta and prostate. Gene expression of CXCL11 is strongly induced by IFN-g and IFN-b, and weakly induced by IFN-a. The I-TAC chemokine elicits its effects on its target cells by interacting with the cell surface chemokine receptor CXCR3, with a higher affinity than do the other ligands for this receptor, CXCL9 and CXCL10. I-TAC is chemotactic for activated T cells. The CXCL11 gene is located on human chromosome 4 along with many other members of the CXC chemokine family.
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Synonyms
Small inducible cytokine B11, CXCL11, I-TAC, IP-9, H174, Beta-R1, chemokine (C-X-C motif) ligand 11, IP9, b-R1, SCYB11, SCYB9B, MGC102770.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized I-TAC although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution I-TAC 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 I-TAC 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
FPMFKRGRCLCIGPGVKAVKVADIEKASIMYPSNNCDKIEVIITLKENKGQRCLNPKSKQARLIIKKVERKNF.
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Background
What is the molecular weight/Mw of CXCL11 HUMAN Protein?
CXCL11 HUMAN Protein has a total Mw of 8.3kDa.
What is the source or expression system of CXCL11 HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL11 HUMAN Protein?
CXCL11 HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL11 HUMAN Protein?
Determined by its ability to chemoattract human IL-2 activated T-Lymphocytes using a concentration range of 0.1-10.0 ng/ml.
What is the amino acid sequence of CXCL11 HUMAN Protein?
FPMFKRGRCLCIGPGVKAVKVADIEKASIMYPSNNCDKIEVIITLKENKGQRCLNPKSKQARLIIKKVERKNF.
What applications can CXCL11 HUMAN Protein be used in?
CXCL11 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL11 HUMAN Protein?
The endotoxin level is minimal, CXCL11 HUMAN Protein was purified using conventional chromatography techniques.
Who supplies recombinant CXCL11 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CXCL11 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ICAM1 Human HEKDescription:
Intercellular Adhesion Molecule-1 Human Recombinant HEK
Intercellular adhesion molecule 1, ICAM-1, Major group rhinovirus receptor, CD54 antigen, ICAM1, BB2, CD54, P3.58.
Product # :
PRO-1643Price :
Quantity :
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Shipped at Room temp
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Description
ICAM1 Human Recombinant produced by mammalian expression system in human cells is a single polypeptide chain containing 461 amino acids (28-480). ICAM1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
ICAM1 was lyophilized from a 0.2 µM filtered solution of 20mM PB and 150mM NaCl, pH 7.2.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
ICAM-1 also called CD54 is a single chain membrane glycoprotein expressed on the surface of a variety of non-haematopoietic and haematopoietic cell types and has roles in signal transduction, cell signaling and lymphocyte adhesion. ICAM1 binds to integrins such as CD11a / CD18, or CD11b / CD18. ICAM1 is also used by Rhinovirus as a receptor. ICAM-1 is an intercellular adhesion molecule constantly present in low concentrations in the membranes of leukocytes and endothelial cells. When stimulated by cytokine the concentrations significantly increase. ICAM-1 can be stimulated by interleukin-1 (IL-1) and tumor necrosis factor alpha (TNFA) and is expressed by the vascular endothelium, macrophages and lymphocytes. ICAM-1 is a ligand for LFA-1 which is a receptor found on leukocytes. Upon activation, leukocytes bind to endothelial cells via ICAM-1/LFA-1 and then transmigrate into tissues.
ICAM-1 is implicated in subarachnoid hemorrhage (SAH). Levels of ICAM-1 are shown to be notably elevated in patients with SAH.
Soluble ICAM-1 is detectable in the plasma and is elevated in patients with various inflammatory conditions. -
Synonyms
Intercellular adhesion molecule 1, ICAM-1, Major group rhinovirus receptor, CD54 antigen, ICAM1, BB2, CD54, P3.58.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized ICAM1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ICAM1 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 ICAM1 in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
QTSVSPSKVILPRGGSVLVTCSTSCDQPKLLGIETPLPKKELLLPGNNRKVYELSNVQE
DSQPMCYSNCPDGQSTAKTFLTVYWTPERVELAPLPSWQPVGKNLTLRCQVEGGAPRANL
TVVLLRGEKELKREPAVGEPAEVTTTVLVRRDHHGANFSCRTELDLRPQGLELFENTSAP
YQLQTFVLPATPPQLVSPRVLEVDTQGTVVCSLDGLFPVSEAQVHLALGDQRLNPTVTYGN
DSFSAKASVSVTAEDEGTQRLTCAVILGNQSQETLQTVTIYSFPAPNVILTKPEVSEGTEV
TVKCEAHPRAKVTLNGVPAQPLGPRAQLLLKATPEDNGRSFSCSATLEVAGQLIHKNQTRELR
VLYGPRLDERDCPGNWTWPENSQQTPMCQAWGNPLPELKCLKDGTFPLPIGESVTVTRDLEGTYL
CRARSTQGEVTRKVTVNVLSPRYEVDHHHHHH.
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 :
SNCA 96-140 HumanDescription:
Alpha Synuclein 96-140 Human Recombinant
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.
Product # :
PRO-164Price :
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Description
A-Synuclein 96-140 Human Recombinant which is a deletion mutant of the a-synuclein amino acids 96-140, produced in E.Coli is a single, non-glycosylated polypeptide chain of 46 amino acids having a molecular mass of 5.2kDa, with an additional Met attached at the N-terminus. The Recombinant Human a-Synuclein 96-140 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SNCA 96-140 protein solution (1mg/ml) contains 20mM Tris-HCl buffer pH 7.5 and 100mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).
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Synonyms
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.
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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
MKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA.
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 :
SNCA A30P HumanDescription:
Alpha Synuclein A30P Human Recombinant
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.
Product # :
PRO-158Price :
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Shipped with Ice Packs
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Description
A-Synuclein A30P Human Recombinant which is a Parkinson’s disease-related point mutant, produced in E.Coli is a single, non-glycosylated polypeptide chain of 140 amino acids having a molecular mass of 14.4kDa (molecular size on SDS-PAGE will appear higher). The Recombinant Human a-Synuclein A30P is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SNCA A30P protein solution (1mg/ml) contains 20mM Tris-HCl buffer pH 7.5 and 100mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).
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Synonyms
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.
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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
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAP GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA.
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 Beta 1a HumanDescription:
IFN-Beta 1a Human Recombinant
Leukocyte IFN, B cell IFN, Type I IFN, IFNB1, IFB, IFF, IFNB, IFN-b 1a ,MGC96956.
Product # :
CYT-236Price :
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Shipped at Room temp
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Description
IFN-beta 1a Human Recombinant produced in CHO (Chinese Hamster Ovarian) cells is a single, glycosylated polypeptide chain containing 166 amino acids and having a molecular mass of 22500 Dalton.IFN-beta1a is purified by proprietary chromatographic techniques.
Source
CHO (Chinese Hamster Ovarian) cells.
Formulation
Lyophilized from a solution containing 91 mg Human Albumin, and 620 mg mannitol and 50mM Acetate acid pH 3.8.
Purity
Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity as determined in a viral resistance assay (human "Wish" cell line and VSV virus or the monkey VERO cell line with EMCV virus) was found to be 270 x 106 IU/mg.Citations
More Info
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Introduction
IFN-beta has antiviral, antibacterial and anticancer activities.
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Synonyms
Leukocyte IFN, B cell IFN, Type I IFN, IFNB1, IFB, IFF, IFNB, IFN-b 1a ,MGC96956.
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Stability
Lyophilized IFN-beta 1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-Beta1a 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 IFN beta 1a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
What is the molecular weight/Mw of IFN BETA 1A HUMAN Protein?
IFN BETA 1A HUMAN Protein has a total Mw of 22.5kDa.
What is the source or expression system of IFN BETA 1A HUMAN Protein?
CHO (Chinese Hamster Ovarian) cells.
What is the Purity of IFN BETA 1A HUMAN Protein?
IFN BETA 1A HUMAN Protein is >99% pure as determined by SDS-PAGE.
What is the Biological Activity of IFN BETA 1A HUMAN Protein?
The specific activity as determined in a viral resistance assay (human "Wish" cell line and VSV virus or the monkey VERO cell line with EMCV virus) was found to be 270 x 106 IU/mg.
What is the amino acid sequence of IFN BETA 1A HUMAN Protein?
IFN BETA 1A HUMAN Protein is composed from 166 amino acids.
What applications can IFN BETA 1A HUMAN Protein be used in?
IFN BETA 1A HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFN BETA 1A HUMAN Protein?
The endotoxin level is minimal, IFN BETA 1A HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SNTN HumanDescription:
Sentan Cilia Apical Structure Protein Human Recombinant
Sentan cilia apical structure protein, FLJ44379, S100AL, S100A1L, S100A-like protein, sentan, S100 calcium-binding protein A1-like.
Product # :
PRO-216Price :
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Shipped with Ice Packs
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Description
SNTN 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 167 amino acids (1-147a.a.) and having a molecular mass of 18.6kDa. The SNTN is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SNTN solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 50% glycerol and 0.15M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
SNTN is a member of to the S-100 family. SNTN is localized solely to the bridging structure between the cell membrane and peripheral singlet microtubules that specifically exists in the narrowed distal portion of cilia. Exogenously expressed sentan displayed affinity for the membrane protrusions, and a protein-lipid binding assay discovered that sentan bounds to phosphatidylserine which indicate that sentan is the leading molecular component of the ciliary tip to link the cell membrane and peripheral singlet microtubules, making the distal portion of the cilia narrow and stiff to permit better airway approval or ovum transport.
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Synonyms
Sentan cilia apical structure protein, FLJ44379, S100AL, S100A1L, S100A-like protein, sentan, S100 calcium-binding protein A1-like.
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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 MGGCMHSTQD KSLHLEGDPN PSAAPTSTCA PRKMPKRISI SKQLASVKAL RKCSDLEKAI ATTALIFRNS SDSDGKLEKA IAKDLLQTQF RNFAEGQETK PKYREILSEL DEHTENKLDF EDFMILLLSI TVMSDLLQNI RNVKIMK
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 :
BACE1 HumanDescription:
Beta-Secretase 1 Human Recombinant
Beta-Secretase, Membrane-Associated Aspartic Protease, Beta-Site APP Cleaving Enzyme, Beta-Site APP-Cleaving Enzyme, Aspartyl Protease, EC 3.4.23.46, Memapsin-2, Asp, BACE, ASP2, Beta-Site Amyloid Beta A4 Precursor Protein-Cleaving Enzyme, Beta-Site Amyloid Precursor Protein Cleaving Enzyme, Transmembrane Aspartic Proteinase Asp2, Beta-Secretase 1 Precursor Variant, Beta-Site APP-Cleaving Enzyme, APP Beta-Secretase, EC 3.4.23, KIAA1149, HSPC104.
Product # :
ENZ-1119Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
BACE1 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 442 amino acids (22-457 a.a.) and having a molecular mass of 49.2kDa. BACE1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
BACE1 protein solution containing Phosphate-Buffered Saline (pH 7.4) containing 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 5 pmol/min/ug in which one unit will convert 1.0 pmole of Mca-SEVNLDAEFRK(Dnp)RR-NH2 to MCA- Pro-Leu-OH per minute at pH 3.5 at 25C.
Citations
More Info
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Introduction
Beta-secretase 1 or BACE1 or beta-site amyloid precursor protein cleaving enzyme 1, is a protein that is encoded by the BACE1 gene in humans. Expression of BACE1 is seen primarily in neurons as it is crucial for the creation of myelin sheats in the peripheric nervous system. Beta-secretase 1 is a proteas that is located in the cell membrane (transmembrane). The enzyme consists of 2 active sites (aspartate residues) in the extracellular domain that can act as a dimer.
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Synonyms
Beta-Secretase, Membrane-Associated Aspartic Protease, Beta-Site APP Cleaving Enzyme, Beta-Site APP-Cleaving Enzyme, Aspartyl Protease, EC 3.4.23.46, Memapsin-2, Asp, BACE, ASP2, Beta-Site Amyloid Beta A4 Precursor Protein-Cleaving Enzyme, Beta-Site Amyloid Precursor Protein Cleaving Enzyme, Transmembrane Aspartic Proteinase Asp2, Beta-Secretase 1 Precursor Variant, Beta-Site APP-Cleaving Enzyme, APP Beta-Secretase, EC 3.4.23, KIAA1149, HSPC104.
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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
TQHGIRLPLR SGLGGAPLGL RLPRETDEEP EEPGRRGSFV EMVDNLRGKS GQGYYVEMTV GSPPQTLNIL VDTGSSNFAV GAAPHPFLHR YYQRQLSSTY RDLRKGVYVP YTQGKWEGEL GTDLVSIPHG PNVTVRANIA AITESDKFFI NGSNWEGILG LAYAEIARPD DSLEPFFDSL VKQTHVPNLF SLQLCGAGFP LNQSEVLASV GGSMIIGGID HSLYTGSLWY TPIRREWYYE VIIVRVEING QDLKMDCKEY NYDKSIVDSG TTNLRLPKKV FEAAVKSIKA ASSTEKFPDG FWLGEQLVCW QAGTTPWNIF PVISLYLMGE VTNQSFRITI LPQQYLRPVE DVATSQDDCY KFAISQSSTG TVMGAVIMEG FYVVFDRARK RIGFAVSACH VHDEFRTAAV EGPFVTLDME DCGYNIPQTD ESTLMTHHHH HH.
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 :
EMAP II HumanDescription:
Endothelial-Monocyte Activating Polypeptide II Human Recombinant
AIMP1, EMAP2, EMAP-2, EMAPII, SCYE1, Multisynthetase complex auxiliary component p43, Endothelial monocyte-activating polypeptide 2, EMAP-II, p43.
Product # :
CYT-607Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
EMAP-II Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 166 amino acids and having a molecular mass of 18.3 kDa. The EMAP-II is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM sodium Phosphate buffer pH=7.5 and 130mM sodium chloride.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by the apoptotic effect on MCF-7 cells using a concentration of 20-30 ng/ml.Citations
More Info
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Introduction
EMAP-II also called SCYE1 is a tumor derived cytokine that plays a role in a wide variety of activities on endothelial cells, monocytes and neutrophils. EMAP-II inhibits endothelial cell proliferation, vasculogenesis, neovessel formation, and can induce apoptosis. It is also chemotactic towards neutrophils and monocytes and induces myeloperoxidase activity from neutrophils. EMAP-II clinical value is inhibiting angiogenesis of vascular beds and suppressing the growth of primary and secondary tumors with no affect to normal tissues. SCYE1is specifically induced by apoptosis, and it is involved in the control of angiogenesis, inflammation, and wound healing. The release of this SCYE1 renders the tumor-associated vasculature sensitive to tumor necrosis factor. The precursor protein is identical to the p43 subunit, which is associated with the multi-tRNA synthetase complex, and it modulates aminoacylation activity of tRNA synthetase in normal cells. EMAP-2 plays a role in in the stimulation of inflammatory responses after proteolytic cleavage in tumor cells.
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Synonyms
AIMP1, EMAP2, EMAP-2, EMAPII, SCYE1, Multisynthetase complex auxiliary component p43, Endothelial monocyte-activating polypeptide 2, EMAP-II, p43.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized EMAP-II although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EMAP-II 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 EMAP-II 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
SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQM QNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.
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Background
What is the molecular weight/Mw of EMAP II HUMAN Protein?
EMAP II HUMAN Protein has a total Mw of 18.3kDa.
What is the source or expression system of EMAP II HUMAN Protein?
Escherichia Coli.
What is the Purity of EMAP II HUMAN Protein?
EMAP II HUMAN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of EMAP II HUMAN Protein?
Determined by the apoptotic effect on MCF-7 cells using a concentration of 20-30 ng/ml.
What is the amino acid sequence of EMAP II HUMAN Protein?
SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQM QNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.
What applications can EMAP II HUMAN Protein be used in?
EMAP II HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EMAP II HUMAN Protein?
The endotoxin level is minimal, EMAP II HUMAN Protein was purified using conventional chromatography techniques
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
OSGEP HumanDescription:
O-Sialoglycoprotein Endopeptidase Human Recombinant
O-Sialoglycoprotein Endopeptidase, T(6)A37 Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, TRNA Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, N6-L-Threonylcarbamoyladenine Synthase, T(6)A Synthase, HOSGEP, GCPL1, Probable TRNA Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, Probable TRNA N6-Adenosine Threonylcarbamoyltransferase , Probable O-Sialoglycoprotein Endopeptidase, EC 3.4.24.57, EC 2.3.1.234, FLJ20411, OSGEP1, PRSMG1, KAE1, Probable tRNA N6-adenosine threonylcarbamoyltransferase.
Product # :
ENZ-821Price :
Quantity :
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Shipped with Ice Packs
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Description
OSGEP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 358 amino acids (1-335 a.a) and having a molecular mass of 38.8kDa. OSGEP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
OSGEP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
O-Sialoglycoprotein Endopeptidase, also known as OSGEP is a member of the KAE1 / TsaD family. OSGEP is essential for the formation of threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs which read codons beginning with adenine. OSGEP take a direct catalytic part in the above reaction, however other proteins of the complex are required to fulfill this activity.
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Synonyms
O-Sialoglycoprotein Endopeptidase, T(6)A37 Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, TRNA Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, N6-L-Threonylcarbamoyladenine Synthase, T(6)A Synthase, HOSGEP, GCPL1, Probable TRNA Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, Probable TRNA N6-Adenosine Threonylcarbamoyltransferase , Probable O-Sialoglycoprotein Endopeptidase, EC 3.4.24.57, EC 2.3.1.234, FLJ20411, OSGEP1, PRSMG1, KAE1, Probable tRNA N6-adenosine threonylcarbamoyltransferase.
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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 MGSMPAVLGF EGSANKIGVG VVRDGKVLAN PRRTYVTPPG TGFLPGDTAR HHRAVILDLL QEALTESGLT SQDIDCIAYT KGPGMGAPLV SVAVVARTVA QLWNKPLVGV NHCIGHIEMG RLITGATSPT VLYVSGGNTQ VIAYSEHRYR IFGETIDIAV GNCLDRFARV LKISNDPSPG YNIEQMAKRG KKLVELPYTV KGMDVSFSGI LSFIEDVAHR MLATGECTPE DLCFSLQETV FAMLVEITER AMAHCGSQEA LIVGGVGCNV RLQEMMATMC QERGARLFAT DERFCIDNGA MIAQAGWEMF RAGHRTPLSD SGVTQRYRTD EVEVTWRD.
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 :
CXCL14 RatDescription:
BRAK (CXCL14) Rat Recombinant
C-X-C motif chemokine 14, B-cell and monocyte-activating chemokine, Chemokine BRAK, Kidney-expressed chemokine CXC, MIP-2G, Small-inducible cytokine B14, Cxcl14, Bmac, Kec, Ks1, Mip2g, Scyb14, BRAK, NJAC, AI414372, bolekine, MIP2gamma, 1110031L23Rik, 1200006I23Rik.
Product # :
CHM-021Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
CXCL14 Rat Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 77 amino acids and having a molecular mass of 9.4kDa.The CXCL14 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CXCL14 was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract activated monocytes using a concentration range of 1.0-10.0 ng/ml.Citations
More Info
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Introduction
CXCL14 is involved in immunoregulatory and inflammatory processes. BRAK protein is structurally related to the CXC (Cys-X-Cys) subfamily of cytokines. CXCL14 displays chemotactic activity for monocytes but not for lymphocytes, dendritic cells, neutrophils or macrophages. CXCL14 is involved in the homeostasis of monocyte-derived macrophages.
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Synonyms
C-X-C motif chemokine 14, B-cell and monocyte-activating chemokine, Chemokine BRAK, Kidney-expressed chemokine CXC, MIP-2G, Small-inducible cytokine B14, Cxcl14, Bmac, Kec, Ks1, Mip2g, Scyb14, BRAK, NJAC, AI414372, bolekine, MIP2gamma, 1110031L23Rik, 1200006I23Rik.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CXCL14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL14 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 CXCL14 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
SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIITTKS MSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE.
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Background
What is the molecular weight/Mw of CXCL14 RAT Protein?
CXCL14 RAT Protein has a total Mw of 9.4kDa.
What is the source or expression system of CXCL14 RAT Protein?
Escherichia Coli.
What is the Purity of CXCL14 RAT Protein?
CXCL14 RAT Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL14 RAT Protein?
Determined by its ability to chemoattract activated monocytes using a concentration range of 1.0-10.0 ng/ml.
What is the amino acid sequence of CXCL14 RAT Protein?
SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIITTKS MSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE.
What applications can CXCL14 RAT Protein be used in?
CXCL14 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL14 RAT Protein?
The endotoxin level is minimal, CXCL14 RAT Protein was purified using conventional chromatography techniques.
Who supplies recombinant CXCL14 RAT that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CXCL14 RAT?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PDGF BB MouseDescription:
Platelet-Derived Growth Factor BB Mouse Recombinant
Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide, Becaplermin.
Product # :
CYT-412Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Platelet-Derived Growth Factor BB Mouse Recombinant produced in E.coli, is a homodimeric, non-glycosylated, polypeptide chain containing 2x110 (total of 2 chains 220aa) amino acids and having a total molecular weight of 24.7 kDa.PDGF-BB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from 10mM NaCitrate pH-3.0.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity is determined by the dose-dependant stimulation of the proliferation of human umbelical vein endothelial cells (HUVEC) using a concentration range of less than 1.6ng/ml.Citations
More Info
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Introduction
PDGF-BB is a member of the platelet-derived growth factor family. The four members of this family are mitogenic factors for cells of mesenchymal origin and are characterized by a motif of eight cysteines. This gene product can exist either as a homodimer (PDGF-BB) or as a heterodimer with the platelet-derived growth factor alpha polypeptide (PDGF-AB), where the dimers are connected by disulfide bonds. Mutations in this gene are associated with meningioma. Reciprocal translocations between chromosomes 22 and 7, at sites where this gene and that for COL1A1 are located, are associated with a particular type of skin tumor called dermatofibrosarcoma protuberans resulting from unregulated expression of growth factor. Two splice variants have been identified for this gene.
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Synonyms
Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide, Becaplermin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Platelet-derived Growth Factor BB although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PDGF BB 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 Platelet-derived Growth Factor-BB in sterile 100mM acetic acid and 0.1% BSA not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MSLGSLAAAE PAVIAECKTR TEVFQISRNL IDRTNANFLV WPPCVEVQRC SGCCNNRNVQ CRASQVQMRP VQVRKIEIVR KKPIFKKATV TLEDHLACKC ETIVTPRPVT
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Background
Platelet-Derived Growth Factor BB (PDGF-BB) is one of the isoforms of the PDGF family that plays a significant role in embryonic development, cell proliferation, cell migration, and angiogenesis.
It's also relevant in the context of certain pathologies like cancer or healing processes.
Here's what a research paper on Mouse Recombinant PDGF-BB might involve:
Basic Biology:
It might discuss the basic biology and function of PDGF-BB in the mouse model. This could include its role in various cellular processes like cell growth, division, and survival, as well as in the context of tissue repair or angiogenesis.
Recombinant PDGF-BB Production:
The paper might describe methods for producing recombinant PDGF-BB in laboratory conditions. It might go into detail on the expression system used (e.g., bacterial, yeast, or mammalian cells), the purification process, and how the functionality of the produced PDGF-BB was confirmed.
Applications:
It could also detail the experimental applications of recombinant PDGF-BB in the mouse model. For instance, it could be used to study wound healing processes, tissue regeneration, or the development and progression of certain diseases.
Comparative Analysis:
The research might include a comparison of the recombinant PDGF-BB with its natural counterpart in terms of functionality, structure, or other properties.
Innovation:
If the paper is presenting new research, it might discuss an innovative use of PDGF-BB, a novel production method, or new findings about its function.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.48 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of PDGF-BB as a Reference Standard.
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 :
CCNA2 HumanDescription:
Cyclin-A2 Human Recombinant
Cyclin-A2, Cyclin-A, CCNA2, CCN1, CCNA.
Product # :
PKA-033Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CCNA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 456 amino acids (1-432 a.a) and having a molecular mass of 51.1kDa.CCNA2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CCNA2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CCNA2 is a member of the highly conserved cyclin family, whose members are characterized by a dramatic periodicity in protein abundance through the cell cycle. Cyclins act as regulators of CDK kinases. Various cyclins demonstrate distinct expression and degradation patterns which contribute to the temporal coordination of each mitotic event. Contrary to cyclin A1, which is present only in germ cells, CCNA2 is expressed in all tissues tested. CCNA2 binds and activates CDC2 or CDK2 kinases, and consequently promotes both cell cycle G1/S and G2/M transitions.
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Synonyms
Cyclin-A2, Cyclin-A, CCNA2, CCN1, CCNA.
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Physical Appearance
Sterile Filtered clear 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 MGSHMLGNSA PGPATREAGS ALLALQQTAL QEDQENINPE KAAPVQQPRT RAALAVLKSG NPRGLAQQQR PKTRRVAPLK DLPVNDEHVT VPPWKANSKQ PAFTIHVDEA EKEAQKKPAE SQKIEREDAL AFNSAISLPG PRKPLVPLDY PMDGSFESPH
TMDMSIVLED EKPVSVNEVP DYHEDIHTYL REMEVKCKPK VGYMKKQPDI TNSMRAILVD WLVEVGEEYK LQNETLHLAV NYIDRFLSSM SVLRGKLQLV GTAAMLLASK FEEIYPPEVA EFVYITDDTY TKKQVLRMEH LVLKVLTFDL AAPTVNQFLT QYFLHQQPAN CKVESLAMFL
GELSLIDADP YLKYLPSVIA GAAFHLALYT VTGQSWPESL IRKTGYTLES LKPCLMDLHQ TYLKAPQHAQ QSIREKYKNS KYHGVSLLNP PETLNL.
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 :
CXCL10 HumanDescription:
IP-10 Human Recombinant (CXCL10)
Small inducible cytokine B10, CXCL10, 10 kDa, Gamma-IP10, IP-10, chemokine (C-X-C motif) ligand 10, C7, IFI10, INP10, crg-2, mob-1, SCYB10, gIP-10.
Product # :
CHM-330Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
IP-10 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 77 amino acids and having a molecular mass of 8.6kDa. The IP-10 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a sterile (0.2 micron) filtered aqueous solution containing 0.1% Trifluoroacetic Acid (TFA).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Chemokine (C-X-C motif) ligand 10 (CXCL10) is a small cytokine belonging to the CXC chemokine family. CXCL10 is secreted by several cell types in response to IFN. These cell types include monocytes, endothelial cells and fibroblasts. CXCL10 has been attributed to several roles, such as chemoattraction for monocytes and T cells, promotion of T cell adhesion to endothelial cells, antitumor activity, and inhibition of bone marrow colony formation and angiogenesis. The gene for CXCL10 is located on human chromosome 4 in a cluster among several other CXC chemokines. This chemokine elicits its effects by binding to the cell surface chemokine receptor CXCR3. The three-dimensional crystal structure of this chemokine has been determined under 3 different conditions to a resolution of up to 1.92A.
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Synonyms
Small inducible cytokine B10, CXCL10, 10 kDa, Gamma-IP10, IP-10, chemokine (C-X-C motif) ligand 10, C7, IFI10, INP10, crg-2, mob-1, SCYB10, gIP-10.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IP-10 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL10 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 IP-10 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
VPLSRTVRCTCISISNQPVNPRSLEKLEIIPASQFCPRVEIIATMKKKGEKRCLNPESKA IKNLLKAVSKERSKRSP.
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Background
What is the molecular weight/Mw of CXCL10 HUMAN Protein?
CXCL10 HUMAN Protein has a total Mw of 8.6kDa.
What is the source or expression system of CXCL10 HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL10 HUMAN Protein?
CXCL10 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL10 HUMAN Protein?
The biological functionality of CXCL10 HUMAN Protein will be determined in the future.
What is the amino acid sequence of CXCL10 HUMAN Protein?
VPLSRTVRCTCISISNQPVNPRSLEKLEIIPASQFCPRVEIIATMKKKGEKRCLNPESKA IKNLLKAVSKERSKRSP.
What applications can CXCL10 HUMAN Protein be used in?
CXCL10 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL10 HUMAN Protein?
The endotoxin level is minimal, CXCL10 HUMAN Protein was purified using conventional chromatography techniques.
Who supplies recombinant CXCL10 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CXCL10 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
PIN1 HumanDescription:
Peptidyl-Prolyl Cis/Trans Isomerase NIMA-Interacting 1 Human Recombinant
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1, EC 5.2.1.8, Rotamase Pin1, PPIase Pin1, DOD, UBL5, PIN1, PPIase.
Product # :
ENZ-331Price :
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Description
PPIase Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids & having a molecular mass of 18.2 kDa. The PIN1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PIN1 protein solution (1 mg/ml) containing 20mM Tris-HCl buffer (pH7.5) 0.1M NaCl, 5mM DTT & 20% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 330 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-HCl pH8.0 using chymotrypsin.Citations
More Info
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Introduction
Human Pin 1 is a peptidyl-prolyl cis/trans isomerase (PPIase) that interacts with NIMA and essential for cell cycle regulation Pin1 is nuclear PPIase containing a WW protein interaction domain, and is structurally and functionally related to Ess1/Ptf1, an essential protein in budding yeast. PPIase activity is necessary for Ess1/Pin1 function in yeast. Pin1 is thus an essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Substrates of Pin1 include the mitotic regulators (Cdc25 phosphatase and NIMA, PLK I, Wee, and Myt1 kinases), several transcription factors like b-Catenin, c-Jun, and the tumor suppressor protein p53, and some specific proteins like the RNA Pol II, the cytoskeleton protein tau, and the G1/S protein Cyclin D1.
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Synonyms
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1, EC 5.2.1.8, Rotamase Pin1, PPIase Pin1, DOD, UBL5, PIN1, PPIase.
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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
MADEEKLPPG WEKRMSRSSG RVYYFNHITN ASQWERPSGN SSSGGKNGQG EPARVRCSHL LVKHSQSRRP SSWRQEKITR TKEEALELIN GYIQKIKSGE EDFESLASQF SDCSSAKARG DLGAFSRGQM QKPFEDASFA LRTGEMSGPV FTDSGIHIIL RTE.
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 :
PLGF1 Human, Sf9Description:
Placental Growth Factor-1 Human Recombinant, Sf9
PIGF, PGF, PLGF-1.
Product # :
CYT-419Price :
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Shipped at Room temp
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Description
Placenta Growth Factor-1 Human Recombinant produced in insect cells is a homodimer, glycosylated polypeptide chain containing 2 x 131 amino acids and having a total molecular mass of approximately 34 kDa. The PLGF-1 is purified by proprietary chromatographic techniques.
Source
Insect Cells.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing 50mM acetic acid.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by its ability to bind to immobilized rh-sFlt-1 in a functional ELISA. PlGF-1 human Recombinant can bind to immobilized rh-sFlt-1 (100ng/well) with a linear range at 0.5-10ng/ml, corresponding to a Specific Activity of 1x105-2x106units/mg.Citations
More Info
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Introduction
PLGF is a growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration. It binds to receptor vegfr-1/flt1.
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Synonyms
PIGF, PGF, PLGF-1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Placenta Growth Factor 1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PLGF1 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 Placenta Growth Factor 1 in sterile 0.1M acetic acid 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 Met-Leu-Pro-Ala-Val.
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 :
LECT1 HumanDescription:
Leukocyte Cell Derived Chemotaxin 1 Human Recombinant
BRICD3, CHM-I, CHM1, MYETS1, Leukocyte cell-derived chemotaxin 1, Chondrosurfactant protein, CH-SP, Chondromodulin-1, ChM-I, LECT1.
Product # :
PRO-1846Price :
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Description
LECT1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 144 amino acids (214-334) and having a molecular mass of 16.3kDa. LECT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LECT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Leukocyte Cell Derived Chemotaxin 1, also known as LECT1, is a glycosylated transmembrane protein which is cleaved to form a mature, secreted protein. The mature protein encourages chondrocyte growth and inhibits angiogenesis. The mature protein takes part in endochondral bone development by permitting cartilaginous anlagen to be vascularized and replaced by bone. LECT1 is expressed in the avascular area of prehypertrophic cartilage and its expression reduces during vascular invasion and chondrocyte hypertrophy.
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Synonyms
BRICD3, CHM-I, CHM1, MYETS1, Leukocyte cell-derived chemotaxin 1, Chondrosurfactant protein, CH-SP, Chondromodulin-1, ChM-I, LECT1.
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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 MGSREVVRKI VPTTTKRPHS GPRSNPGAGR LNNETRPSVQ EDSQAFNPDN PYHQQEGESM TFDPRLDHEG ICCIECRRSY THCQKICEPL GGYYPWPYNY QGCRSACRVI MPCSWWVARI LGMV.
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 :
LINGO1 HumanDescription:
Leucine Rich Repeat And Ig Domain Containing 1 Human Recombinant
Leucine Rich Repeat And Ig Domain Containing 1, LRRN6A, Leucine-Rich Repeat And Immunoglobulin Domain-Containing Protein 1, Leucine-Rich Repeat Neuronal Protein 1, Leucine Rich Repeat Neuronal 6A, LERN1, Leucine-Rich Repeat And Immunoglobulin-Like Domain-Containing Nogo Receptor-Interacting Protein 1, Leucine-Rich Repeat Neuronal Protein 6A, UNQ201, LERN1, Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1.
Product # :
PRO-2187Price :
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Description
LINGO1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 133 amino acids (241-337 a.a) and having a molecular mass of 15.1kDa. LINGO1 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LINGO1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Leucine Rich Repeat And Ig Domain Containing 1, also known as Lingo1 is primarily expressed in neuronal tissue, and most abundantly in the cortex. In addition, Lingo 1 is involved in the inhibition of axon regeneration all the way through a ternary complex formed with NgR1 (ligand-binding subunit) and p75 (signal transducing subunit). The inhibitory action is accomplished through RhoA-GTP upregulation in response to the presence of MOG, MAG or Nogo-66 in the central nervous system. Furthermore, LINGO-1 inhibits oligodendrocyte precursor differentiation as well as myelination, by a mechanism which also involves activation of RhoA, however it appears that it does not require 75 or NgR1.
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Synonyms
Leucine Rich Repeat And Ig Domain Containing 1, LRRN6A, Leucine-Rich Repeat And Immunoglobulin Domain-Containing Protein 1, Leucine-Rich Repeat Neuronal Protein 1, Leucine Rich Repeat Neuronal 6A, LERN1, Leucine-Rich Repeat And Immunoglobulin-Like Domain-Containing Nogo Receptor-Interacting Protein 1, Leucine-Rich Repeat Neuronal Protein 6A, UNQ201, LERN1, Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSLKVL EISHWPYLDT MTPNCLYGLN LTSLSITHCN LTAVPYLAVR HLVYLRFLNL SYNPISTIEG SMLHELLRLQ EIQLVGGQLA VVEPYAFRGL NYL.
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 :
GOT1 MouseDescription:
Glutamic-Oxaloacetic Transaminase 1 Mouse Recombinant
Aspartate aminotransferase, cytoplasmic, cAspAT, Cysteine aminotransferase, cytoplasmic, Cysteine transaminase, cytoplasmic, cCAT, Glutamate oxaloacetate transaminase 1, Transaminase A.
Product # :
ENZ-872Price :
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Description
GOT1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 436 amino acids (1-413a.a) and having a molecular mass of 48.6kDa.GOT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GOT1 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
GOT1 is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, which participate in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and show close homology.
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Synonyms
Aspartate aminotransferase, cytoplasmic, cAspAT, Cysteine aminotransferase, cytoplasmic, Cysteine transaminase, cytoplasmic, cCAT, Glutamate oxaloacetate transaminase 1, Transaminase A.
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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 MGSMAPPSVF AQVPQAPPVL VFKLTADFRD DPDPRKVNLG VGAYRTDESQ PWVLPVVRKV EQKIANDNSL NHEYLPILGL AEFRSCASRL VLGDNSPAIR ENRVGGVQSL GGTGALRIGA DFLGRWYNGT DNKNTPIYVS SPTWENHNAV FSAAGFKDIR PYCYWDAEKR GLDLQGFLND LENAPEFSIF VLHACAHNPT GTDPTPEQWK QIAAVMQRRF LFPFFDSAYQ GFASGDLEKD AWAIRYFVSE GFELFCAQSF SKNFGLYNER VGNLTVVGKE SDSVLRVLSQ MEKIVRITWS NPPAQGARIV AATLSDPELF KEWKGNVKTM ADRILTMRSE LRARLEALKT PGTWSHITEQ IGMFSFTGLN PKQVEYLVNE KHIYLLPSGR INMCGLTTKN LDYVATSIHE AVTKIQ.
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 :
CNTF RatDescription:
Ciliary Neurotrophic Factor Rat Recombinant
HCNTF, CNTF, Ciliary Neurotrophic Factor.
Product # :
CYT-654Price :
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Shipped at Room temp
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Description
CNTF Recombinant Rat produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids and having a molecular mass of 22834 Dalton. The CNTF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 0.025% NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Analysis by Gel Filtration.
(b) Analysis by SDS-PAGE.Biological Activity
Fully biologically active by its ability to phosphorylate STAT3 in several cells lines.Citations
More Info
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Introduction
CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy. -
Synonyms
HCNTF, CNTF, Ciliary Neurotrophic Factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CNTF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CNTF 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 CNTF in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in presence of carrier protein.
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Amino Acid Sequence
AFAEQTPLTL HRRDLSSRSIWLARKIRSDLTALMESYVKHQGLNKNI
NLDSVDGVPVASTDRWSEMTEAERLQENLQAYRTFQGMLTKLLEDQRV
HFTPTEGDFHQAIHTLMLQVSAFAYQLEELMVLLEQKIPENEADGMPA
TVGDGGLFEKKLWGLKVLQELSQWTVRSIHDLRVISSHQMGISALESH
YGAKDKQM. -
Background
What is the molecular weight/Mw of CNTF Protein?
CNTF Protein has a total Mw of 22kDa.
What is the source or expression system of CNTF Protein?
Escherichia Coli.
What is the Purity of CNTF Protein?
CNTF Protein is >99% pure as determined by SDS-PAGE.
What is the Biological Activity of CNTF Protein?
Fully biologically active by its ability to phosphorylate STAT3 in several cells lines.
What is the amino acid sequence of CNTF Protein?
AFAEQTPLTL HRRDLSSRSIWLARKIRSDLTALMESYVKHQGLNKNI
NLDSVDGVPVASTDRWSEMTEAERLQENLQAYRTFQGMLTKLLEDQRV
HFTPTEGDFHQAIHTLMLQVSAFAYQLEELMVLLEQKIPENEADGMPA
TVGDGGLFEKKLWGLKVLQELSQWTVRSIHDLRVISSHQMGISALESH YGAKDKQM.
What applications can CNTF Protein be used in?
CNTF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CNTF Protein?
The endotoxin level is minimal, CNTF 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 :
CCL7 HumanDescription:
Monocyte Chemotactic Protein-3 Human Recombinant (CCL7)
Small inducible cytokine A7, CCL7, Monocyte chemotactic protein 3, MCP-3, Monocyte chemoattractant protein 3, NC28, chemokine (C-C motif) ligand 7, FIC, MARC, MCP3, SCYA6, SCYA7, MGC138463, MGC138465.
Product # :
CHM-317Price :
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Description
Monocyte Chemotactic Protein-3 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 76 amino acids and having a molecular mass of 9011 Dalton. The MCP-3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity as determined by the ability of MCP-3 to chemoattract human peripheral blood at 8 - 80ng/ml corresponding to a Specific Activity of 12,500-125,000IU/mg.Citations
More Info
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Introduction
Chemokine (C-C motif) ligand 7 (CCL7) is a small cytokine known as a chemokine that was previously called monocyte-specific chemokine 3 (MCP3). Due to CCL7 possessing two adjacent N-terminal cysteine residues in its mature protein, it is classified among the subfamily of chemokines known as CC chemokines. CCL7 specifically attracts monocytes, and regulates macrophage function. It is produced by certain tumor cell lines and by macrophages. This chemokine is located on chromosome 17 in humans, in a large cluster containing many other CC chemokines and is most closely related to CCL2(previously called MCP1).
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Synonyms
Small inducible cytokine A7, CCL7, Monocyte chemotactic protein 3, MCP-3, Monocyte chemoattractant protein 3, NC28, chemokine (C-C motif) ligand 7, FIC, MARC, MCP3, SCYA6, SCYA7, MGC138463, MGC138465.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MCP-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL7 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 Monocyte Chemotactic Protein-3in 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 Gln-Pro-Val-Gly-Ile.
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Background
What is the molecular weight/Mw of CCL7 HUMAN Protein?
CCL7 HUMAN Protein has a total Mw of 9.01kDa.
What is the source or expression system of CCL7 HUMAN Protein?
Escherichia Coli.
What is the Purity of CCL7 HUMAN Protein?
CCL7 HUMAN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL7 HUMAN Protein?
The specific activity as determined by the ability of MCP-3 to chemoattract human peripheral blood at 8 - 80ng/ml corresponding to a Specific Activity of 12,500-125,000IU/mg.
What is the amino acid sequence of CCL7 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Gln-Pro-Val-Gly-Ile.
What applications can CCL7 HUMAN Protein be used in?
CCL7 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL7 HUMAN Protein?
The endotoxin level is minimal, CCL7 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CRABP2 HumanDescription:
Cellular Retinoic Acid binding Protein 2 Human Recombinant
RBP6, CRABP-II, CRABP2, RETINOIC ACID-BINDING PROTEIN CELLULAR TYPE II, Cellular retinoic acid-binding protein 2, Cellular retinoic acid-binding protein II.
Product # :
PRO-637Price :
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Description
CRABP2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 136 amino acids and having a molecular mass of 15.6 kDa. The CRABP2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CRABP2 protein solution contains 20mM Tris-HCl pH-8 and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CRABP2 NCBI Accession No: NP_001869 regulates the access of retinoic acid to the nuclear retinoic acid receptors. CRABP2 is involved in a regulatory feedback mechanism that controls the action of retinoic acid on cell differentiation.
CRABP2 is involved in the conversion of vitamin A into its intracellular active form retinoic acid, which regulate the genes responsible for lipid metabolism and adipocyte differentiation. CRABP2 gene is located on chromosome 1q21-23 and this region has been linked with related disorders such as familial combined hyperlipidemia (FCHL) and type 2 diabetes mellitus.
CRABP proteins are of low molecular weight having an important function in retinoic acid-mediated regulation of human skin growth and differentiation. -
Synonyms
RBP6, CRABP-II, CRABP2, RETINOIC ACID-BINDING PROTEIN CELLULAR TYPE II, Cellular retinoic acid-binding protein 2, Cellular retinoic acid-binding protein II.
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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
MPNFSGNWKI IRSENFEELL KVLGVNVMLR KIAVAAASKP AVEIKQEGDT FYIKTSTTVR TTEINFKVGE EFEEQTVDGR PCKSLVKWES ENKMVCEQKL LKGEGPKTSW TRELTNDGEL ILTMTADDVV CTRVYVRE.
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.