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1000 results found for “Cyclin”
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Name :
CXCL1 HumanDescription:
GRO-Alpha Human Recombinant (CXCL1)
Growth-regulated protein alpha, CXCL1, Melanoma growth stimulatory activity, MGSA, Neutrophil-activating protein 3, NAP-3, GRO-alpha (1-73), chemokine (C-X-C motif) ligand 1, GRO1, GROa, SCYB1, MGSA-a, MGSA alpha.
Product # :
CHM-329Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
GRO Alpha Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7811 Dalton. The GRO-alpha is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in 20mM PB, pH 7.4, 50mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.
More Info
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Introduction
Chemokine (C-X-C motif) ligand 1 (CXCL1) is a small cytokine belonging to the CXC chemokine family that was previously called GRO1 oncogene, Neutrophil-activating protein 3 (NAP-3) and melanoma growth stimulating activity, alpha (MSGA-a). It is secreted by human melanoma cells, has mitogenic properties and is implicated in melanoma pathogenesis. CXCL1 is expressed by macrophages, neutrophilsand epithelial cells, and has neutrophil chemoattractant activity. CXCL1 plays a role in spinal cord development by inhibiting the migration of oligodendrocyte precursors and is involved in the processes of angiogenesis, inflammation, wound healing, and tumorigenesis. This chemokine elicits its effects by signaling through the chemokine receptor CXCR2. The gene for CXCL1 is located on human chromosome 4 amongst genes for other CXC chemokines.
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Synonyms
Growth-regulated protein alpha, CXCL1, Melanoma growth stimulatory activity, MGSA, Neutrophil-activating protein 3, NAP-3, GRO-alpha (1-73), chemokine (C-X-C motif) ligand 1, GRO1, GROa, SCYB1, MGSA-a, MGSA alpha.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GRO-alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL1 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CXCL1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ser-Val-Ala-Thr.
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Background
What is the molecular weight/Mw of CXCL1 HUMAN Protein?
CXCL1 HUMAN Protein has a total Mw of 7.81kDa.
What is the source or expression system of CXCL1 HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL1 HUMAN Protein?
CXCL1 HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL1 HUMAN Protein?
Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.
What is the amino acid sequence of CXCL1 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ser-Val-Ala-Thr.
What applications can CXCL1 HUMAN Protein be used in?
CXCL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL1 HUMAN Protein?
The endotoxin level is minimal, CXCL1 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
LYN HumanDescription:
v-yes-1 Yamaguchi Sarcoma Viral Related Oncogene Human Recombinant
Tyrosine-protein kinase Lyn, Lck/Yes-related novel protein tyrosine kinase, V-yes-1 Yamaguchi sarcoma viral related oncogene homolog, p53Lyn, p56Lyn, JTK8, EC 2.7.10, LYN Proto-Oncogene, Src Family Tyrosine Kinase, V-Yes-1 Yamaguchi Sarcoma Viral Related Oncogene Homolog, Lck/Yes-Related Novel Protein Tyrosine Kinase, EC 2.7.10.2.
Product # :
PRO-136Price :
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Description
LYN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 535 amino acids (1-512) and having a molecular mass of 61.0kDa. LYN is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The LYN solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) ,0.4M urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Tyrosine-protein kinase Lyn (LYN) belongs to the src family of non-receptor protein tyrosine kinases, which is primarily expressed in haematopoietic tissues. LYN protein is involved in induction of stress-activated protein kinase (SAPK), but not ERK or p38 MAPK, in response to genotoxic agents. LYN protein stimulates SAPK by a MKK7- and MEKK1-dependent mechanism. The LYN - MEKK1 - MKK7 - SAPK pathway is efficient in the induction of apoptosis by genotoxic agents.
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Synonyms
Tyrosine-protein kinase Lyn, Lck/Yes-related novel protein tyrosine kinase, V-yes-1 Yamaguchi sarcoma viral related oncogene homolog, p53Lyn, p56Lyn, JTK8, EC 2.7.10, LYN Proto-Oncogene, Src Family Tyrosine Kinase, V-Yes-1 Yamaguchi Sarcoma Viral Related Oncogene Homolog, Lck/Yes-Related Novel Protein Tyrosine Kinase, EC 2.7.10.2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMGCIKSK GKDSLSDDGV DLKTQPVRNT ERTIYVRDPT SNKQQRPVPE SQLLPGQRFQ TKDPEEQGDI VVALYPYDGI HPDDLSFKKG EKMKVLEEHG EWWKAKSLLT KKEGFIPSNY VAKLNTLETE EWFFKDITRK DAERQLLAPG NSAGAFLIRE SETLKGSFSL SVRDFDPVHG DVIKHYKIRS LDNGGYYISP RITFPCISDM IKHYQKQADG LCRRLEKACI SPKPQKPWDK DAWEIPRESI KLVKRLGAGQ FGEVWMGYYN NSTKVAVKTL KPGTMSVQAF LEEANLMKTL QHDKLVRLYA VVTREEPIYI ITEYMAKGSL LDFLKSDEGG KVLLPKLIDF SAQIAEGMAY IERKNYIHRD LRAANVLVSE SLMCKIADFG LARVIEDNEY TAREGAKFPI KWTAPEAINF GCFTIKSDVW SFGILLYEIV TYGKIPYPGR TNADVMTALS QGYRMPRVEN CPDELYDIMK MCWKEKAEER PTFDYLQSVL DDFYTATEGQ YQQQP.
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 :
VAMP3 HumanDescription:
Synaptobrevin-3 Human Recombinant
VAMP3, VAMP-3, Cellubrevin, Vesicle-Associated Membrane Protein 3, Synaptobrevin-3, CEB, SYB3.
Product # :
PRO-652Price :
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Shipped with Ice Packs
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Description
VAMP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8.7 kDa.
Source
Escherichia Coli.
Formulation
The VAMP3 protein solution contains 20mM Tris pH-7.5 and 10% glycerol.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
VAMP3 is present in recycling endosomes and endosome-derived vesicles. VAMP3 has been implicated in recycling of transferrin receptors to the plasma membrane, secretion of alpha-granules in platelets, recycling of T-cell receptors to the immunological synapses, and membrane trafficking during cell migration. VAMP-3 is present in human platelets and necessary for granule secretion. Synaptobrevins are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. VAMP3 high homology to other VAMPs in its broad tissue distribution and subcellular localization is shown to be the human equivalent of the rodent cellubrevin. In platelets the protein resides on a compartment that is not mobilized to the plasma membrane on calcium or thrombin stimulation.
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Synonyms
VAMP3, VAMP-3, Cellubrevin, Vesicle-Associated Membrane Protein 3, Synaptobrevin-3, CEB, SYB3.
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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
MSTGPTAATG SNRRLQQTQN QVDEVVDIMR VNVDKVLERD QKLSELDDRA DALQAGASQF ETSAAKLKRK YWWKNCK.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
VAMP8 HumanDescription:
Endobrevin Human Recombinant
VAMP8, VAMP-8, Endobrevin, Vesicle-Associated Membrane Protein 8, EDB.
Product # :
PRO-660Price :
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Description
VAMP8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 96 amino acids (1-76 a.a.) and having a molecular mass of 10.9 kDa. The VAMP8 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatography techniques.
Source
Escherichia Coli.
Formulation
The VAMP8 protein solution (0.25mg/ml) contains 20mM Tris pH-8, 0.1mM PMSF, 0.2M NaCl and 50% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
VAMP8 also called endobrevin, is the main component of a SNARE complex involved in the docking and fusion of synaptic vesicles with the presynaptic membrane. VAMP8 protein is involved in the regulatation of enzyme secretion in pancreatic acinar cells and plays a part in the abscission of the midbody during cell division, which leads to completely separate daughter cells. VAMP8 is essential for dense-granule secretion in platelets. VAMP8 is related with the perinuclear vesicular structures of the early endocytic compartment. VAMP8 interacts particularly with the soluble NSF-attachment protein (alpha-SNAP), through an VAMP8-containing SNARE complex.
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Synonyms
VAMP8, VAMP-8, Endobrevin, Vesicle-Associated Membrane Protein 8, EDB.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MEEASEGGGN DRVRNLQSEV EGVKNIMTQN VERILARGEN LEHLRNKTED LEATSEHFKT TSQKVARKFW WKNVKM.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MAP1LC3B2 HumanDescription:
Microtubule-Associated Protein 1 Light Chain 3 Beta 2 Human Recombinant
Microtubule-associated proteins 1A/1B light chain 3 beta 2, Microtubule-associated proteins 1A/1B light chain 3B-like, MAP1LC3B2, ATG8G.
Product # :
PRO-215Price :
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Shipped with Ice Packs
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Description
MAP1LC3B2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 140 amino acids (1-120 a.a.) and having a molecular mass of 16.2kDa.MAP1LC3B2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MAP1LC3B2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Microtubule-associated proteins 1A/1B light chain 3 beta 2 (MAP1LC3B2) is a member of the MAP1LC3 family. MAP1LC3B2 is a subunit of neuronal microtubule-associated MAP1A and MAP1B proteins, which are involved in microtubule assembly and essential for neurogenesis. The MAP1LC3B2 protein is possibly involved in formation of autophagosomal vacuoles (autophagosomes). MAP1LC3B2 is expressed primarily in the heart, testis, brain and skeletal muscle.
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Synonyms
Microtubule-associated proteins 1A/1B light chain 3 beta 2, Microtubule-associated proteins 1A/1B light chain 3B-like, MAP1LC3B2, ATG8G.
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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 MPSEKTFKQR RTFEQRVEDV RLIREQHPTK IPVIIERYKG EKQLPVLDKT KFLVPDHVNM SELIKIIRRR LQLNANQAFF LLVNGHSMVS VSTPISEVYE SEKDEDGFLY MVCASQETFG.
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 :
SCGN RatDescription:
Secretagogin Rat Recombinant
SCGN, EF-hand calcium binding protein, Setagin, SEGN, CALBL, Secretagogin.
Product # :
PRO-657Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Secretagogin Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 286 amino acids and having a molecular mass of 33.3 kDa. The Rat SCGN is fused to a 10 a.a. His tag at N-Terminus.The protein’s amino acids sequence is identical to UniProtKB/Swiss-Prot entry Q6R556.The Rat SCGN is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The sterile filtered concentrated protein solution was lyophilized with 20mM Tris & 50mM NaCl pH-7.5.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
SCGN is a secreted calcium-binding protein which is found in the cytoplasm. It is related to calbindin D-28K and calretinin. Secretagogin is involved in KCL-stimulated calcium flux and cell proliferation.
Secretagogin plays a role in human non-functional pituitary adenomas. -
Synonyms
SCGN, EF-hand calcium binding protein, Setagin, SEGN, CALBL, Secretagogin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.
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Solubility
Add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely.
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Amino Acid Sequence
MKHHHHHHAS MDNAHRQTQA HLDAACFWQI WQRFDKDEKG YIKETELDAF FDDLLAKFGI EDTLMEENVQ KMKEQLMVGH DISKEGRILM KELASMFLSE DENFLLFFRL ETPLDNSVEF MQIWRKYDAD SSGFISAAEL SNFLRDLFLH HKKVISEAEL EEYTSTMMKI FDRNKDGRLD LNDLARILAL QENFLLQFKM DASSTEERKR DFEKIFAHYD VSKTGALEGP EVDGFVKDMM ELVQPSISGV DLDKFREILL RHCDVNKDGK IQKSELALCLGLKINP.
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 :
DYNLRB1 HumanDescription:
Dynein Light Chain Roadblock-Type 1 Human Recombinant
BITH, BLP, DNCL2A, DNLC2A, ROBLD1, HSPC162.
Product # :
PRO-489Price :
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Shipped with Ice Packs
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Description
DYNLRB1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 104 amino acids (1-96 a.a.) and having a molecular mass of 11.9 kDa. The DYNLRB1 is fused to an 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DYNLRB1 protein solution (1mg/ml) containing 20mM Tris-HCl pH-8 & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Dynein light chain roadblock-type (DYNLRB1) belongs to the roadblock dynein light chain family and encodes a cytoplasmic protein which is capable of binding intermediate chain proteins. Upregulation of the DYNLRB1 gene is linked with hepatocellular carcinomas, suggesting that DYNLRB1 may be involved in tumor progression.
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Synonyms
BITH, BLP, DNCL2A, DNLC2A, ROBLD1, HSPC162.
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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
MAEVEETLKR LQSQKGVQGI IVVNTEGIPI KSTMDNPTTT QYASLMHSFI LKARSTVRDI DPQNDLTFLR IRSKKNEIMV APDKDYFLIV IQNPTELEHH 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 :
BCL2L11 HumanDescription:
BCL2 Like 11 Human Recombinant
Bcl-2-like protein 11, Bcl2-L-11, Bcl2-interacting mediator of cell death, BCL2L11, BIM, BAM, BOD.
Product # :
PRO-1171Price :
Quantity :
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Shipped with Ice Packs
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Description
BCL2L11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 162 amino acids (1-138 a.a) and having a molecular mass of 18.5kDa.BCL2L11 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
BCL2L11 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer, pH8.0, 2M Urea, 20% glycerol, 5mM DTT and 300mM NaCl.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
Bcl-2-like protein 11 (BCL2L11) is a member of the Bcl-2 family and contains a Bcl-2 homology domain 3 (BH3). BCL2L11 expression can be stimulated by nerve growth factor (NGF), in addition to the forkhead transcription factor (FKHR-L1) which proposes a role of the BCL2L11 gene in neuronal and lymphocyte apoptosis. BCL2L11 interacts with other members of the BCL-2 protein family, including BCL2, BCL2L1/BCL-X(L), and MCL1, and acts as an apoptotic activator. BimEL, BimL and BimS are the main isoforms which are ubiquitously expressed with a tissue-specific variation. The Isoform Bim-gamma, on the other hand, is most abundantly expressed in the small intestine and colon, and in lower levels in spleen, prostate, testis, heart, liver and kidney.
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Synonyms
Bcl-2-like protein 11, Bcl2-L-11, Bcl2-interacting mediator of cell death, BCL2L11, BIM, BAM, BOD.
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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 MGSHMAKQPS DVSSECDREG RQLQPAERPP QLRPGAPTSL QTEPQDRSPA PMSCDKSTQT PSPPCQAFNH YLSAMASMRQ AEPADMRPEI WIAQELRRIG DEFNAYYARR VFLNNYQAAE DHPRMVILRL LRYIVRLVWR MH.
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 :
KLRK1 Human, Sf9Description:
Killer Cell lectin-Like Receptor Subfamily K, Member 1 Human Recombinant, Sf9
Killer Cell Lectin Like Receptor K1, Killer Cell Lectin-Like Receptor Subfamily K, Member 1, NKG2-D-Activating NK Receptor, NK Cell Receptor D, D12S2489E, NKG2D, DNA Segment On Chromosome 12 (Unique) 2489 Expressed Sequence, Killer Cell Lectin-Like Receptor Subfamily K Member 1, NKG2-D Type II Integral Membrane Protein, CD314 Antigen, NKG2-D, CD314, KLR.
Product # :
PRO-2474Price :
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Description
KLRK1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 386 amino acids (73-216a.a.) and having a molecular mass of 43.9kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). KLRK1 is expressed with a 242 amino acids hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
KLRK1 protein solution (0.5mg/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
Killer Cell lectin-Like Receptor Subfamily K, Member 1 (KLRK1) is an activating receptor which has recently generated considerable interest. The most fascinating of these, are a couple of closely related proteins known as MICA and MICB. These are cell-surface molecules distantly related to MHC class I proteins, and their genes have elements of heat shock promoters. Thus, MICA and MICB are expressed in the course of cell stress and are up-regulated in tumor cells and during viral infections. This receptor-ligand combination has a crucial role in the immune response to various pathologies.
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Synonyms
Killer Cell Lectin Like Receptor K1, Killer Cell Lectin-Like Receptor Subfamily K, Member 1, NKG2-D-Activating NK Receptor, NK Cell Receptor D, D12S2489E, NKG2D, DNA Segment On Chromosome 12 (Unique) 2489 Expressed Sequence, Killer Cell Lectin-Like Receptor Subfamily K Member 1, NKG2-D Type II Integral Membrane Protein, CD314 Antigen, NKG2-D, CD314, KLR.
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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
ADPIWSAVFL NSLFNQEVQI PLTESYCGPC PKNWICYKNN CYQFFDESKN WYESQASCMS QNASLLKVYS KEDQDLLKLV KSYHWMGLVH IPTNGSWQWE DGSILSPNLL TIIEMQKGDC ALYASSFKGY IENCSTPNTY ICMQRTVVEP 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 :
Clusterin MouseDescription:
Apolipoprotein-J Mouse Recombinant
CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.
Product # :
CYT-1172Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Clusterin Mouse Recombinant is a single, glycosylated polypeptide chain containing 433 amino acids (22-448a.a) and having a molecular mass of 50.2kDa (calculated). Clusterin is fused to a 6 a.a His tag at C-terminal.
Source
HEK293
Formulation
Clusterin filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20 mM Tris buffer and 50 mM NaCl, pH 7.5.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Clusterin also known as Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by 5 disulfide bridges and are flanked by 2 predicted coiled-coil a-helices and 3 predicted amphipathic a-helices.
Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% -80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, heparin, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
Clusterin is up/down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others. -
Synonyms
CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely.
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Amino Acid Sequence
EQEVSDNELQ ELSTQGSRYI NKEIQNAVQG VKHIKTLIEK TNAERKSLLN SLEEAKKKKE DALEDTRDSE MKLKAFPEVC NETMMALWEE CKPCLKHTCM KFYARVCRSG SGLVGQQLEE FLNQSSPFYF WMNGDRIDSL LESDRQQSQV LDAMQDSFAR ASGIIDTLFQ DRFFARELHD PHYFSPIGFP HKRPHFLYPK SRLVRSLMSP SHYGPPSFHN MFQPFFEMIH QAQQAMDVQL HSPAFQFPDV DFLREGEDDR TVCKEIRRNS TGCLKMKGQC EKCQEILSVD CSTNNPAQAN LRQELNDSLQ VAERLTEQYK ELLQSFQSKM LNTSSLLEQL NDQFNWVSQL ANLTQGEDKY YLRVSTVTTH SSDSEVPSRV TEVVVKLFDS DPITVVLPEE VSKDNPKFMD TVAEKALQEY RRKSRAEHHH HHH
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Background
What is the molecular weight/Mw of CLUSTERIN Protein?
CLUSTERIN Protein has a total Mw of 50.2kDa.
What is the source or expression system of CLUSTERIN Protein?
HEK293
What is the Purity of CLUSTERIN Protein?
CLUSTERIN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CLUSTERIN Protein?
The biological functionality of CLUSTERIN Protein will be determined in the future.
What is the amino acid sequence of CLUSTERIN Protein?
EQEVSDNELQ ELSTQGSRYI NKEIQNAVQG VKHIKTLIEK TNAERKSLLN SLEEAKKKKE DALEDTRDSE MKLKAFPEVC NETMMALWEE CKPCLKHTCM KFYARVCRSG SGLVGQQLEE FLNQSSPFYF WMNGDRIDSL LESDRQQSQV LDAMQDSFAR ASGIIDTLFQ DRFFARELHD PHYFSPIGFP HKRPHFLYPK SRLVRSLMSP SHYGPPSFHN MFQPFFEMIH QAQQAMDVQL HSPAFQFPDV DFLREGEDDR TVCKEIRRNS TGCLKMKGQC EKCQEILSVD CSTNNPAQAN LRQELNDSLQ VAERLTEQYK ELLQSFQSKM LNTSSLLEQL NDQFNWVSQL ANLTQGEDKY YLRVSTVTTH SSDSEVPSRV TEVVVKLFDS DPITVVLPEE VSKDNPKFMD TVAEKALQEY RRKSRAEHHH HHH
What applications can CLUSTERIN Protein be used in?
CLUSTERIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CLUSTERIN Protein?
The endotoxin level is minimal, CLUSTERIN 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 :
RAB3IL1 HumanDescription:
RAB3A Interacting Protein Like 1 Human Recombinant
GRAB, Rab-3A-interacting-like protein 1, Guanine nucleotide exchange factor for Rab-3A, Rab3A-interacting-like protein 1, Rabin3-like 1.
Product # :
PRO-2141Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
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- More Info
Description
RAB3IL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 405 amino acids (1-382a.a) and having a molecular mass of 45kDa.RAB3IL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RAB3IL1 protein solution (0.25mg/ml) containing Phosphate buffer saline (pH 7.4) and 50% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
RAB3A Interacting Protein Like 1 (RAB3IL1) is a 382 amino acid protein which is a member of the SEC2 family. RAB3IL1 is a guanine nucleotide exchange factor (GEF) for Rab3A. RAB3IL1 competes for interaction with Rab3A and IHPK1 via its coiled coil domain, which doesn’t involve IHPK1 kinase activity.
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Synonyms
GRAB, Rab-3A-interacting-like protein 1, Guanine nucleotide exchange factor for Rab-3A, Rab3A-interacting-like protein 1, Rabin3-like 1.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMWSGPPQ PDQGLPPPLA AVPVPWKSTD PCQGHRESPG ALVETSAGEE AQGQEGPAAA QLDVLRLRSS SMEIREKGSE FLKEELHRAQ KELKLKDEEC ERLSKVREQL EQELEELTAS LFEEAHKMVR EANMKQAASE KQLKEARGKI DMLQAEVTAL KTLVITSTPA SPNRELHPQL LSPTKAGPRK GHSRHKSTSS TLCPAVCPAA GHTLTPDREG KEVDTILFAE FQAWRESPTL DKTCPFLERV YREDVGPCLD FTMQELSVLV RAAVEDNTLT IEPVASQTLP TVKVAEVDCS STNTCALSGL TRTCRHRIRL GDSKSHYYIS PSSRARITAV CNFFTYIRYI QQGLVRQDAE PMFWEIMRLR KEMSLAKLGF FPQEA.
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 :
NCR2 HumanDescription:
Natural Cytotoxicity Triggering Receptor 2 Human Recombinant
Natural Cytotoxicity Triggering Receptor 2, Lymphocyte Antigen 95 (Activating NK-Receptor; NK-P44), Natural Killer Cell P44-Related Protein, NK Cell-Activating Receptor, Lymphocyte Antigen 95 Homolog, CD336 Antigen, NK-p44, LY95, dJ149M18.1.
Product # :
PRO-1826Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NCR2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 133 amino acids (19-130) and having a molecular mass of 15.0 kDa. NCR2 is fused to a 21 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The NCR2 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
-
Introduction
NCR2 is a member of the natural cytotoxicity receptor (NCR) family and holds 1 immunoglobulin-like (Ig-like) domain. NCR2 cooperates with TYROBP/DAP12 and is specifically expressed by activated NK cells and by in vitro cultured TCRg/d lymphoid cells. NCR2 is a cytotoxicity-activating receptor which induces the amplified efficiency of activated natural killer (NK) cells to mediate tumor cell lysis.
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Synonyms
Natural Cytotoxicity Triggering Receptor 2, Lymphocyte Antigen 95 (Activating NK-Receptor; NK-P44), Natural Killer Cell P44-Related Protein, NK Cell-Activating Receptor, Lymphocyte Antigen 95 Homolog, CD336 Antigen, NK-p44, LY95, dJ149M18.1.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSQAQSKAQV LQSVAGQTLT VRCQYPPTGS LYEKKGWCKE ASALVCIRLV TSSKPRTMAW TSRFTIWDDP DAGFFTVTMT DLREEDSGHY WCRIYRPSDN SVSKSVRFYL VVS
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 :
Eotaxin HumanDescription:
Eotaxin Human Recombinant (CCL11)
Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.
Product # :
CHM-256Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Eotaxin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 74 amino acids and having a molecular mass of 8345.9 Dalton. The CCL11 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 20mM PB, pH 7.4, 150mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity is determined by the chemoattract of human PBE (peripheral blood eosinophils) at a concentration between 0.1-10 ng/ml corresponding to a Specific Activity of 100,000-10,000,000IU/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, MGC22554.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Eotaxin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL11 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 Eotaxin Human Recombinant 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
GPASVPTTCC FNLANRKIPL QRLESYRRIT SGKCPQKAVI FKTKLAKDICADPKKKWVQD
SMKYLDQKSP TPKP.
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Background
What is the molecular weight/Mw of EOTAXIN HUMAN Protein?
EOTAXIN HUMAN Protein has a total Mw of 8.3459kDa.
What is the source or expression system of EOTAXIN HUMAN Protein?
Escherichia Coli.
What is the Purity of EOTAXIN HUMAN Protein?
EOTAXIN HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of EOTAXIN HUMAN Protein?
The activity is determined by the chemoattract of human PBE (peripheral blood eosinophils) at a concentration between 0.1-10 ng/ml corresponding to a Specific Activity of 100,000-10,000,000IU/mg.
What is the amino acid sequence of EOTAXIN HUMAN Protein?
GPASVPTTCC FNLANRKIPL QRLESYRRIT SGKCPQKAVI FKTKLAKDICADPKKKWVQD
SMKYLDQKSP TPKP.
What applications can EOTAXIN HUMAN Protein be used in?
EOTAXIN HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EOTAXIN HUMAN Protein?
The endotoxin level is minimal, EOTAXIN 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.
- View Data Sheet
Name :
FAM49B HumanDescription:
Family with Sequence Similarity 49, Member B Human Recombinant
BM-009, L1, Protein FAM49B, FAM49B.
Product # :
PRO-1411Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
FAM49B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 347amino acids (1-324 a.a) and having a molecular mass of 39.1kDa. FAM49B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
FAM49B protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
Family with Sequence Similarity 49, Member B (FAM49B) is a member of the FAM49 family. In the latest genome-wide transcriptional analysis, a gene signature was identified for multiple sclerosis (MS), which reverted back to normal during pregnancy. The reversion was mostly evident for seven genes: SOCS2, TNFAIP3, NR4A2, CXCR4, POLR2J, FAM49B, and STAG3L1, most of which are negative regulators of inflammation.
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Synonyms
BM-009, L1, Protein FAM49B, FAM49B.
-
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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMGNLLKV LTCTDLEQGP NFFLDFENAQ PTESEKEIYN QVNVVLKDAE GILEDLQSYR GAGHEIREAI QHPADEKLQE KAWGAVVPLV GKLKKFYEFS QRLEAALRGL LGALTSTPYS PTQHLEREQA LAKQFAEILH FTLRFDELKM TNPAIQNDFS YYRRTLSRMR INNVPAEGEN EVNNELANRM SLFYAEATPM LKTLSDATTK FVSENKNLPI ENTTDCLSTM ASVCRVMLET PEYRSRFTNE ETVSFCLRVM VGVIILYDHV HPVGAFAKTS KIDMKGCIKV LKDQPPNSVE GLLNALRYTT KHLNDETTSK QIKSMLQ.
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 :
GADD45G HumanDescription:
Growth Arrest and DNA-Damage-Inducible Gamma Human Recombinant
DDIT2, GADD45gamma, GADD45G, Growth arrest and DNA-damage-inducible protein GADD45 gamma, Cytokine-responsive protein CR6, DNA-damage-inducible transcript 2, DDIT-2, CR6, GRP17.
Product # :
PRO-570Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- purity
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Description
GADD45G Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 159 amino acids and having a molecular mass of 17.1 kDa.
Source
Escherichia Coli.
Formulation
The GADD45G protein solution (1mg/ml) contains 20mM Tris-HCl pH-7.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
GADD45G is part of the nuclear proteins to interact with various proteins whose transcript levels are raised after stressful growth arrest conditions and treatment with DNA-damaging agents. GADD45G reacts to environmental stresses by mediating activation of the p38/JNK pathway which is mediated through their protein binding and activating MTK1/MEKK4 kinase, which is an upstream activator of both p38 and JNK MAPKs. GADD45G acts as a new-age tumor suppressor however is being frequently inactivated epigenetically in multiple tumors. GADD45G mRNA expression is down-regulated in hepatocellular carcinoma. GADD45G causes cell cycle arrest at G2/M transition when transfected into Hep-G2 cells. GADD45 Gamma induction by androgens involves new protein synthesis. Overexpression of GADD45 Gamma inhibits cell growth and causes morphological modifications in prostate cell lines thus GADD45 gamma takes part in differentiation induction by androgens.
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Synonyms
DDIT2, GADD45gamma, GADD45G, Growth arrest and DNA-damage-inducible protein GADD45 gamma, Cytokine-responsive protein CR6, DNA-damage-inducible transcript 2, DDIT-2, CR6, GRP17.
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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
MTLEEVRGQD TVPESTARMQ GAGKALHELL LSAQRQGCLT AGVYESAKVL NVDPDNVTFC VLAAGEEDEG DIALQIHFTL IQAFCCENDIDIVRVGDVQR LAAIVGAGEE AGAPGDLHCI LISNPNEDAW KDPALEKLSL FCEESRSVND WVPSITLPE.
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 Receptor ChickenDescription:
Leptin Receptor Chicken Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor, Leptin Receptor.
Product # :
CYT-509Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Leptin Binding Domain Chicken Recombinant also called Leptin Receptor produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 208 amino acids and having a molecular mass of 24.5 kDa. Chicken Leptin Receptor consists of the cytokine binding domain of leptin receptor amino acids 420-626 of chicken leptin receptor.The Leptin Binding Domain is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was filter sterilized and stored at 4°C (0.2 to 0.5 mg/ml) solution of Tris-HCl buffer, pH 9.0 with 150mM NaCl.
Purity
Greater than 99.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
Leptin Receptor is a part of the gp130 family of cytokine receptors that stimulate gene transcription by activating cytosolic STAT proteins. Leptin Receptor plays a role in the regulation of fat metabolism and in novel hematopoietic pathway that is obligatory for normal lymphopoiesis. Leptin Receptorparticipates in the regulation of counter-regulatory response to hypoglycemia by inhibiting neurons of the parabrachial nucleus.Leptin Receptoraffectsspecifically on T lymphocyte responses.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor, Leptin Receptor.
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Physical Appearance
Sterile Filtered colorless solution at a concentration of 0.4 mg/ml.
-
Stability
Sterile solutions at 0.5mg/ml or less are stable at 4°C for several months.
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Amino Acid Sequence
The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Ile-Asp-Val-Asn-Ile Biological ActivityBiological Activity is evidenced by high affinity binding of mammalian leptins at 1:1 molar ratio.
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Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 2.45 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 calibrated solution of Leptin Binding Domain 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.
- View Data Sheet
Name :
Leptin tA Human, PEGDescription:
Leptin Antagonist Triple Mutant Human Recombinant, Pegylated
Product # :
CYT-702Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- biological activity
- More Info
Description
Pegylated Leptin Antagonist Triple Mutant Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular weight of 35.6kDa, Leptin was mutated, resulting in L39A/D40A/F41A. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 200 kDa protein. Leptin Antagonist Triple Mutant Human Recombinant is Mono-Pegylated with 20kDa PEG and was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein 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
Capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is 6-8 fold lower than the non-pegylated antagonist but in vivo it has profound weight gain effect (as compared to the non-pegylated antagonist), resulting mainly from increased food intake. Its in vivo activity compared to that of PEG-MLA is 9-27 fold higher.More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized PEG-SHLA although stable at room temperature for several weeks, should be stored desiccated below - 20C. Upon reconstitution at > 0.1 mg/ml and up to 2 mg/ml of PEG-SHLA and filter sterilization mLEP mutant can be stored at 4C 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 pegylated Human Recombinant in sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 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.
- View Data Sheet
Name :
CFLAR HumanDescription:
CASP8 and FADD-Like Apoptosis Regulator Human Recombinant
CASP8 and FADD-like apoptosis regulator, CASH, CLARP, Casper, I-FLICE, Inhibitor of FLICE, MRIT, c-FLIP, FLAME, FLAME-1, FADD-like antiapoptotic molecule 1, Caspase homolog, Caspase-eight-related protein, Caspase-like apoptosis regulatory protein, Cellular FLICE-like inhibitory protein, CASP8AP1, MACH-related inducer of toxicity, usurpin beta, CASPER.
Product # :
PRO-920Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
CFLAR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 480 amino acids (1-480) and having a molecular mass of 55.3 kDa.The CFLAR is purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CFLAR solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
The precise role of CFLAR is not yet revealed but it seems it is vital in apoptosis regulation downstream of all identified death receptors.
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Synonyms
CASP8 and FADD-like apoptosis regulator, CASH, CLARP, Casper, I-FLICE, Inhibitor of FLICE, MRIT, c-FLIP, FLAME, FLAME-1, FADD-like antiapoptotic molecule 1, Caspase homolog, Caspase-eight-related protein, Caspase-like apoptosis regulatory protein, Cellular FLICE-like inhibitory protein, CASP8AP1, MACH-related inducer of toxicity, usurpin beta, CASPER.
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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
MSAEVIHQVE EALDTDEKEM LLFLCRDVAI DVVPPNVRDL LDILRERGKL SVGDLAELLY RVRRFDLLKR ILKMDRKAVE THLLRNPHLV SDYRVLMAEI GEDLDKSDVS SLIFLMKDYM GRGKISKEKS FLDLVVELEK LNLVAPDQLD LLEKCLKNIH RIDLKTKIQK YKQSVQGAGT SYRNVLQAAI QKSLKDPSNN FRLHNGRSKE QRLKEQLGAQ QEPVKKSIQE SEAFLPQSIP EERYKMKSKP LGICLIIDCI GNETELLRDT FTSLGYEVQK FLHLSMHGIS QILGQFACMP EHRDYDSFVC VLVSRGGSQS VYGVDQTHSG LPLHHIRRMF MGDSCPYLAG KPKMFFIQNY VVSEGQLENS SLLEVDGPAM KNVEFKAQKR GLCTVHREAD FFWSLCTADM SLLEQSHSSP SLYLQCLSQK LRQERKRPLL DLHIELNGYM YDWNSRVSAK EKYYVWLQHT LRKKLILSYT.
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 :
PSMD10 HumanDescription:
Gankyrin Human Recombinant
26S proteasome non-ATPase regulatory subunit 10, 26S proteasome regulatory subunit p28, Gankyrin, PSMD10, p28, dJ889N15.2.
Product # :
ENZ-404Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
- formulation
- purity
- More Info
Description
PSMD10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 226 amino acids and having a molecular mass of 24.4 kDa.
Source
Escherichia Coli.
Formulation
The PSMD10 protein solution (1mg/ml) contains 1x PBS pH-7.4 & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Gankyrin (proteasome 26S subunit) is a multicatalytic proteinase oncoprotein commonly overexpressed in most hepatocellular carcinomas. Proteasomes are found throughout eukaryotic cells at a high concentrations and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. Gankyrin interacts with S6 ATPase of the 19S regulatory particle of the 26S proteasome. Gankyrin is involved in theregulation of the phosphorylation of the retinoblastoma protein by CDK4, and to enhance the ubiquitinylation of p53 by MDM2. Gankyrin consists of 7 ankyrin repeats and is structurally similar to I kappa Bs. Gankyrin acts as a regulatory subunit of the 26s proteasome which is involved in the atp-dependent degradation of ubiquitinated proteins. Gankyrin is involved in progression of esophageal squamous cell carcinoma. gankyrin plays an oncogenic role especially in early stages of human epatocarcinogenesis. Gankyrin binds to NF-kappaB and suppresses its activity at the transcription level by modulating acetylation through SIRT1. Structural comparison between Gankyrin & p16(INK4A) identified numerous residues of gankyrin that are potentially important for CDK4 binding.
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Synonyms
26S proteasome non-ATPase regulatory subunit 10, 26S proteasome regulatory subunit p28, Gankyrin, PSMD10, p28, dJ889N15.2.
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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
MEGCVSNLMV CNLAYSGKLE ELKESILADK SLATRTDQDS RTALHWACSA GHTEIVEFLL QLGVPVNDKD DAGWSPLHIA ASAGRDEIVK ALLGKGAQVN AVNQNGCTPL HYAASKNRHE IAVMLLEGGA NPDAKDHYEA TAMHRAAAKG NLKMIHILLY YKASTNIQDT EGNTPLHLAC DEERVEEAKL LVSQGASIYI ENKEEKTPLQ VAKGGLGLIL KRMVEG.
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 :
CTF2P MouseDescription:
Neuropoietin Mouse Recombinant
Cardiotrophin-2, CT-2, Neuropoietin, Np, Ctf2, Gm494.
Product # :
CYT-1128Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
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Description
Neuropoietin Mouse Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 182 amino acids and having a molecular mass of approximately 19.7kDa.CTF2P is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in 20mM Tris-HCl, pH 8.0, 0.5mM DTT and 500mM NaCl.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by a cell proliferation assay using human TF-1 cells is < 200 ng/ml, corresponding to a specific activity of > 5000 IU/mg.
More Info
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Introduction
CTF2P, aka Neuropoietinis a part of the IL-6 family of cytokines. CTF2P is the outcome of a gene duplication event involving cardiotrophin-1 (CT-1) and it helps to define a subfamily within the IL-6 family that includes CT-1, CLC and CTNF. CTF2P Increases the platelet count associated with splenomegaly and takes part in neuronal precursor development and maturation.
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Synonyms
Cardiotrophin-2, CT-2, Neuropoietin, Np, Ctf2, Gm494.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CTF2P although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Neuropoietin 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 Neuropoietin in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
APISPSEPIG QAYSLALYMQ KNTSALLQTY LQHQGSPFSD PGFSAPELQL STLPSAAVSF KTWHAMEDAE RLSRAQGAFL ALTQHLQLVG DDQSYLNPGS PILLAQLGAA RLRAQGLLGN MAAIMTALGL PIPPEEDTLG FVPFGASAFE RKCRGYIVTR EYGHWTDRAV RDLALLKAKY SA.
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Background
What is the molecular weight/Mw of CTF2P Protein?
CTF2P Protein has a total Mw of 19.7kDa.
What is the source or expression system of CTF2P Protein?
Escherichia Coli.
What is the Purity of CTF2P Protein?
CTF2P Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of CTF2P Protein?
The ED50 as determined by a cell proliferation assay using human TF-1 cells is < 200 ng/ml, corresponding to a specific activity of > 5000 IU/mg.
What is the amino acid sequence of CTF2P Protein?
APISPSEPIG QAYSLALYMQ KNTSALLQTY LQHQGSPFSD PGFSAPELQL STLPSAAVSF KTWHAMEDAE RLSRAQGAFL ALTQHLQLVG DDQSYLNPGS PILLAQLGAA RLRAQGLLGN MAAIMTALGL PIPPEEDTLG FVPFGASAFE RKCRGYIVTR EYGHWTDRAV RDLALLKAKY SA.
What applications can CTF2P Protein be used in?
CTF2P Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CTF2P Protein?
The endotoxin level is minimal, CTF2P 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 :
TRIM21 Human BiotinDescription:
Tripartite Motif Containing 21 (RO52) Human Recombinant, Biotinylated
52 kDa Ro protein, Sjoegren syndrome type A antigen, SS-A, Ro(SS-A), 52 kDa ribonucleoprotein autoantigen Ro/SS-A, Tripartite motif-containing protein 21, RING finger protein 81, TRIM21, RNF81, RO52, SSA1, SSA, RO-52.
Product # :
PRO-2559Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TRIM21 Human Recombinant, Biotin produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 52kDa. TRIM21 is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
TRIM21 solution is supplied in 20mM HEPES pH-7.6, 0.01mM EDTA and 0.02% SDS.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
TRIM21 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The 52 kDa Ro protein is part of the RoSSA ribonucleoprotein, which includes a single polypeptide and one of four small RNA molecules. The RoSSA particle localizes to both the cytoplasm and the nucleus. Ro/SSA interacts with autoantigens in patients with Sjogren syndrome and systemic lupus erythematosus. Ribonucleoprotein particle is composed of a single polypeptide and one of four small RNA molecules. The RoSSA is present in all mammalian cells studied but has no known function. At least 2 isoforms are present in nucleated and red blood cells, and tissue specific differences in Ro/SSA proteins were identified.
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Synonyms
52 kDa Ro protein, Sjoegren syndrome type A antigen, SS-A, Ro(SS-A), 52 kDa ribonucleoprotein autoantigen Ro/SS-A, Tripartite motif-containing protein 21, RING finger protein 81, TRIM21, RNF81, RO52, SSA1, SSA, RO-52.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG type human auto antibodies.2. Functional Streptavidin based ELISA test (analysis of positive/negative samples.)
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 :
Activin B Human ActiveDescription:
Activin-B Human Recombinant, Active
Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.
Product # :
CYT-057Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Activin B human Recombinant produced in Nicotiana benthamiana plant is a beta-B single chain (aa 293-406) containing 123 amino acids (molecular formula C615H910N178O177S12). Activin B is fused to a 10-His-tag at the N-terminal having the total molecular mass of 14kDa and purified by standard chromatographic techniques.
Source
Nicotiana benthamiana plant
Formulation
Lyophilized from 1mg/ml solution in 0.05M Tris-HCl buffer pH 7.4.
Purity
Greater than 97.0% as determined by Analysis by SDS-PAGE.
Biological Activity
The biological activity of Activin B is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation. EC50 <5ng/ml is required to stimulate a half-maximal response at cytokine saturation. Note: Since applications vary, each investigator should titrate the reagent to obtain optimal results.More Info
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Synonyms
Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Activin B although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin B 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 Activin B 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
HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG.
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Background
An Investigation into the Functional Roles and Therapeutic Potential of Activin-B Human Recombinant, Active
1. Abstract
Activin-B Human Recombinant, Active, also referred to as beta-2, Activin beta-B chain, or MGC157939, is a crucial component of the Transforming Growth Factor-beta (TGF-beta) superfamily. The multifaceted nature of this protein implicates it in numerous physiological processes. This paper delves into the bioactivity of Activin-B, exploring its role in cellular proliferation, differentiation, apoptosis, and its potential for therapeutic applications, especially in the realms of regenerative medicine, reproductive health, and cancer therapy.
2. Introduction
The TGF-beta superfamily, of which Activin-B is a member, is renowned for its far-reaching implications in cell and developmental biology. This superfamily boasts members that control cell growth, differentiation, and apoptosis, thus playing vital roles in organogenesis, bone growth, and reproductive functions. This research paper aims to shed light on the characteristics and potential therapeutic applications of Activin-B.
3. Structure and Synthesis of Activin-B
Activin-B is a dimeric protein, composed of two identical beta-B chains. This homodimer undergoes multiple stages of synthesis, starting as a precursor protein, which then experiences proteolytic processing to eventually form the mature peptide. It is this coordinated activity of various enzymes and molecular chaperones that ensure the accurate biosynthesis of Activin-B.
4. Biological Functions of Activin-B
Activin-B's roles extend from embryogenesis and organogenesis to the modulation of reproductive functions. Its influence over cellular proliferation, differentiation, and apoptosis has significant repercussions in physiological and pathological scenarios. Its regulatory functions also encompass immunomodulation and wound healing, underpinning its extensive biological reach.
5. Activin-B in Regenerative Medicine
Regenerative medicine's primary focus is the repair and regeneration of tissues, and it is here that the potential of Activin-B shines. The protein's capacity to regulate cellular processes positions it as a possible agent in tissue repair, making it an intriguing research topic for therapeutic applications in regenerative medicine.
6. Activin-B and Reproductive Health
Activin-B’s role in reproductive health is undeniable, having been implicated in follicular development, ovulation, and pregnancy maintenance. Its potent influence on reproductive functions indicates the possibility of its use in the treatment of reproductive disorders, providing a potential pathway for further therapeutic development.
7. Activin-B in Cancer
Recent research has connected the deregulation of Activin-B to various types of cancer. Deciphering the mechanisms through which Activin-B affects cancer cell proliferation and survival could open up new avenues for targeted cancer therapy. This critical linkage emphasizes the need for comprehensive studies on Activin-B's role in oncogenesis.
8. Conclusion and Future Perspectives
Our understanding of Activin-B's biological functions has grown immensely, but many mysteries remain. The continued exploration of the molecular mechanisms through which Activin-B operates will undoubtedly yield more insights into its potential therapeutic uses, guiding the development of new treatments for a myriad of diseases.
What is the molecular weight / Mw of Activin B Protein?
Activin A Protein has a total Mw of 14 kDa.What is the source or expression system of Activin B Protein?
Nicotinia
What is the Purity of Activin B Protein?
Activin B Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of Activin B Protein?
The biological activity of Activin B is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation. EC50 <5ng/ml is required to stimulate a half-maximal response at cytokine saturation. Note: Since applications vary, each investigator should titrate the reagent to obtain optimal results.
What is the endotoxin level for Activin B Protein?
The endotoxin level is minimal, ACTIVIN B Protein was purified using conventional chromatography techniques.
What is the amino acid sequence of ACTIVIN B Protein?
HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG
What applications can ACTIVIN B Protein be used in?
ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.
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 :
ATF1 HumanDescription:
Activating Transcription Factor-1 Human Recombinant
Activating transcription factor 1, cyclic AMP-dependent transcription factor ATF-1, Protein TREB36, EWS-ATF1, FUS/ATF-1.
Product # :
PKA-019Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
ATF1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 295 amino acids (1-271 and having a molecular mass of 31.8kDa.ATF1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ATF1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 5mM DTT, 2mM EDTA and 50% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
ATF1, a cyclic-AMP dependent transcription factor, is expressed in a large selection of cell types and can dimerize with CREB. MSK1 and MSK2 protein kinases are essential for the stress-induced phosphorylation of transcription factors CREB and ATF1 in primary embryonic fibroblasts. Epidermal growth factor induction of c-jun expression needs ATF1 and MEF2 sites in the c-jun promoter.
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Synonyms
Activating transcription factor 1, cyclic AMP-dependent transcription factor ATF-1, Protein TREB36, EWS-ATF1, FUS/ATF-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
MGSSHHHHHH SSGLVPRGSH MGSHMEDSHK STTSETAPQP GSAVQGAHIS HIAQQVSSLS ESEESQDSSD SIGSSQKAHG ILARRPSYRK ILKDLSSEDT RGRKGDGENS GVSAAVTSMS VPTPIYQTSS GQYIAIAPNG ALQLASPGTD GVQGLQTLTM TNSGSTQQGT TILQYAQTSD GQQILVPSNQ VVVQTASGDM QTYQIRTTPS ATSLPQTVVM TSPVTLTSQT TKTDDPQLKR EIRLMKNREA ARECRRKKKE YVKCLENRVA VLENQNKTLI EELKTLKDLY SNKSV
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 :
OSM Human, 209 a.aDescription:
Oncostatin M Human Recombinant (209 a.a.)
OSM, MGC20461, Oncostatin M.
Product # :
CYT-639Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
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Description
Oncostatin-M (209 a.a.) Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 209 amino acids and having a molecular mass of 23.9kDa. The Oncostatin-M (209 a.a.) is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Oncostatin-M (209 a.a.) was lyophilized from a concentrated (1mg/ml) solution containing 1x PBS pH-7.4.
Purity
Greater than 97.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of Human TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000 IU/mg.More Info
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Introduction
Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.
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Synonyms
OSM, MGC20461, Oncostatin M.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Oncostatin-M (209 a.a.) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Oncostatin-M (209 a.a.) 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 Oncostatin-M (209 a.a.) 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
AAIGSCSKEYRVLLGQLQKQTDLMQDTSRLLDPYIRIQGLDVPKLREHCRERPG
AFPSEETLRGLGRRGFLQTLNATLGCVLHRLADLEQRLPKAQDLERSGLNIEDL
EKLQMARPNILGLRNNIYCMAQLLDNSDTAEPTKAGRGASQPPTPTPASDAFQ
RKLEGCRFLHGYHRFMHSVGRVFKWGESPNRSRRHSPHQALRKGVRR.
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.