Search: 1000 results found for "macrophage migration inhibitory factor"

Description:

IFN-Beta 1b Human Recombinant

Leukocyte IFN, B cell IFN, Type I IFN, IFNB1, IFB, IFF, IFNB, IFN-b 1b, MGC96956.

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CYT-234

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Description

IFN beta 1b Human Recombinant produced in E.Coli is a single, non-glycosylated mutein (variant form) of human IFN beta-1b polypeptide chain containing 165 amino acids and having a molecular mass of 18510.86 Dalton.The IFN-beta gene was cloned from human fibroblasts and altered to substitute Serine for the Cysteine residue found at position 17. IFN beta-1b is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from 1mg/ml solution containing 50mg Human Albumin & 50mg dextrose.

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 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 32 x 10⁶ IU/mg.

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Introduction
IFN-beta 1b has antiviral, antibacterial and anticancer activities.
Synonyms
Leukocyte IFN, B cell IFN, Type I IFN, IFNB1, IFB, IFF, IFNB, IFN-b 1b, MGC96956.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IFN-beta 1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFNB 1b should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IFN beta-1b in sterile 18M-cm H2O at a concentration of 0.25mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Tyr-Asn-Leu-Leu.
Background
What is the molecular weight/Mw of IFN BETA 1B HUMAN Protein?
IFN BETA 1B HUMAN Protein has a total Mw of 18.5kDa.

What is the source or expression system of IFN BETA 1B HUMAN Protein?
Escherichia Coli.

What is the Purity of IFN BETA 1B HUMAN Protein?
IFN BETA 1B HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IFN BETA 1B 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 32 x 106 IU/mg.

What is the amino acid sequence of IFN BETA 1B HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Tyr-Asn-Leu-Leu.

What applications can IFN BETA 1B HUMAN Protein be used in?
IFN BETA 1B HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFN BETA 1B HUMAN Protein?
The endotoxin level is minimal, IFN BETA 1B HUMAN Protein was purified using conventional chromatography techniques.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.493 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 IFN-beta 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.

Description:

IFN Gamma Receptor 1 Human Recombinant

IFNGR1, CD119, IFNGR, IMD27A, IMD27B, CDw119.

Product # :

CYT-1074

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Description

IFNGR1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 234 amino acids (18-245a.a.) and having a molecular mass of 26.6kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions).IFNGR1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IFNGR1 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
IFNGR1 is a part of the hematopoietic cytokine receptor superfamily. IFNGR1 forms a site that is recognized by the extracellular domain of IFNGR2 by inducing the rapid dimerization of chains. IFNGR1 Plays an important role in the IFN-gamma pathway that is essential for the cellular response to infectious agents. IFNGR1 is expressed in a membrane-bound form in various cells, and is over-expressed in tumor cells.
Synonyms
IFNGR1, CD119, IFNGR, IMD27A, IMD27B, CDw119.
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
EMGTADLGPS SVPTPTNVTI ESYNMNPIVY WEYQIMPQVP VFTVEVKNYG VKNSEWIDAC INISHHYCNI SDHVGDPSNS LWVRVKARVG QKESAYAKSE EFAVCRDGKI GPPKLDIRKE EKQIMIDIFH PSVFVNGDEQ EVDYDPETTC YIRVYNVYVR MNGSEIQYKI LTQKEDDCDE IQCQLAIPVS SLNSQYCVSA EGVLHVWGVT TEKSKEVCIT IFNSSIKGHH HHHH.
Background
What is the molecular weight/Mw of IFNGR1 HUMAN Protein?
IFNGR1 HUMAN Protein has a total Mw of 16.8kDa.

What is the source or expression system of IFNGR1 HUMAN Protein?
Escherichia Coli.

What is the Purity of IFNGR1 HUMAN Protein?
IFNGR1 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IFNGR1 HUMAN Protein?
The ED50 as determined by an anti-viral assay using human HeLa cells infected with encephalomyocarditis (EMC) virus is < 20.0 ng/ml, corresponding to a specific activity of > 5.0 × 104 IU/mg.

What is the amino acid sequence of IFNGR1 HUMAN Protein?
QDPYVKEAEN LKKYFNAGDP DVADNGTLFL DILRNWKEES DRKIMQSQIV SFYFKLFKNF KDDQRIQKSV ETIKEDINVK FFNSNKKKRD DFEKLTNYSV TDSNVQRKAV HELIQVMAEL SPAAKIGKRK RSQMFRGRRA SQ.

What applications can IFNGR1 HUMAN Protein be used in?
IFNGR1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFNGR1 HUMAN Protein?
The endotoxin level is minimal, IFNGR1 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.

Description:

Serine Peptidase Inhibitor Kazal Type 7 Human Recombinant

Serine peptidase inhibitor Kazal type 7, ECG2, ECRG2, Serine protease inhibitor Kazal-type 7, Esophagus cancer-related gene 2 protein, ECRG-2, SPINK7.

Product # :

PRO-1507

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Description

SPINK7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 89 amino acids (20-85) and having a molecular mass of 9.6 kDa.SPINK7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The SPINK7 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol and 2mM DTT.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Serine peptidase inhibitor Kazal type 7 (SPINK7) which includes one Kazal-like domain is most likely serine protease inhibitor. Diseases linked with SPINK7 include esophageal cancer, and oral squamous cell carcinoma
Synonyms
Serine peptidase inhibitor Kazal type 7, ECG2, ECRG2, Serine protease inhibitor Kazal-type 7, Esophagus cancer-related gene 2 protein, ECRG-2, SPINK7.
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 MGSSEAASLS PKKVDCSIYK KYPVVAIPCP ITYLPVCGSD YITYGNECHL CTESLKSNGR VQFLHDGSC.

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.

Description:

Calcium Modulating Ligand Human Recombinant

Calcium Modulating Ligand, Calcium-Modulating Cyclophilin Ligand, Calcium-Signal Modulating Cyclophilin Ligand, Cyclophilin B-Binding Protein, CAML.

Product # :

PRO-1612

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Description

CAMLG Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-189) and having a molecular mass of 23.2kDa.CAMLG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CAMLG solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
CAMLG binds to cyclophilin B and operates downstream of the TCR and upstream of calcineurin by causing an influx of calcium. CAMLG is an essential membrane protein that takes part in the calcium signal transduction pathway, connecting cyclophilin B to calcium signaling.
Synonyms
Calcium Modulating Ligand, Calcium-Modulating Cyclophilin Ligand, Calcium-Signal Modulating Cyclophilin Ligand, Cyclophilin B-Binding Protein, CAML.
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 MGSMESMAVA TDGGERPGVP AGSGLSASQR RAELRRRKLL MNSEQRINRI MGFHRPGSGA EEESQTKSKQ QDSDKLNSLS VPSVSKRVVL GDSVSTGTTD QQGGVAEVKG TQLGDKLDSF IKPPECSSDV NLELRQRNRG DLTADSVQRG SRHGLEQYLS RFEEAMKLRK QLISEKPSQE DGNTTEEFDS FR

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.

Description:

Peptidase Inhibitor 3 Human Recombinant

Peptidase Inhibitor 3 Skin-Derived, Skin-Derived Antileukoproteinase, Protease Inhibitor 3 Skin-Derived (SKALP), WAP Four-Disulfide Core Domain Protein 14, WAP Four-Disulfide Core Domain 14, Elastase-Specific Inhibitor, Protease Inhibitor WAP3, ESI, trappin-2, cementoin, WFDC14, WAP3, elafin, pre-elafin, SKALP, Peptidase Inhibitor 3.

Product # :

PRO-1627

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Description

PI3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 118 amino acids (23-117) and having a molecular mass of 12.0kDa.PI3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PI3 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 80% as determined by SDS-PAGE.

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Introduction
PI3 is an elastase-specific protease inhibitor, which contains a WAP-type four-disulfide core (WFDC) domain, and is thus a member of the WFDC domain family. Most WFDC gene members are localized to chromosome 20q12-q13 in two clusters: centromeric and telomeric. PI3 belongs to the centromeric cluster.
Synonyms
Peptidase Inhibitor 3 Skin-Derived, Skin-Derived Antileukoproteinase, Protease Inhibitor 3 Skin-Derived (SKALP), WAP Four-Disulfide Core Domain Protein 14, WAP Four-Disulfide Core Domain 14, Elastase-Specific Inhibitor, Protease Inhibitor WAP3, ESI, trappin-2, cementoin, WFDC14, WAP3, elafin, pre-elafin, SKALP, Peptidase Inhibitor 3.
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 MGSAVTGVPV KGQDTVKGRV PFNGQDPVKG QVSVKGQDKV KAQEPVKGPV STKPGSCPII LIRCAMLNPP NRCLKDTDCP GIKKCCEGSC GMACFVPQ

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.

Description:

Mitogen-Activated Protein Kinase 12 Human Recombinant

Mitogen-activated protein kinase 12, SAPK3, ERK6, PRKM12, Extracellular signal-regulated kinase 6, Mitogen-activated protein kinase p38 gamma, Stress-activated protein kinase 3, MAP kinase 12, MAP kinase p38 gamma, MAPK 12, ERK3, p38gamma, EC 2.7.11.24, EC 2.7.11.

Product # :

PKA-015

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Description

MAPK12 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 387 amino acids (1-367 a.a.) and having a molecular mass of 44.1kDa.MAPK12 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MAPK12 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 100mM NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE analysis.

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Introduction
MAPK12 is a member of the MAP kinase family. MAPK12 acts as a signal transducer during differentiation of myoblasts to myotubes. p38 proteins utilizes magnesium as a cofactor to catalyze the ATP-dependent phosphorylation of target proteins and is produced in several regions all over the body with common expression patterns in heart.
Synonyms
Mitogen-activated protein kinase 12, SAPK3, ERK6, PRKM12, Extracellular signal-regulated kinase 6, Mitogen-activated protein kinase p38 gamma, Stress-activated protein kinase 3, MAP kinase 12, MAP kinase p38 gamma, MAPK 12, ERK3, p38gamma, EC 2.7.11.24, EC 2.7.11.
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 MSSPPPARSG FYRQEVTKTA WEVRAVYRDL QPVGSGAYGA VCSAVDGRTG AKVAIKKLYR PFQSELFAKR AYRELRLLKH MRHENVIGLL DVFTPDETLD DFTDFYLVMP FMGTDLGKLM KHEKLGEDRI QFLVYQMLKG LRYIHAAGII HRDLKPGNLA VNEDCELKIL DFGLARQADS EMTGYVVTRW YRAPEVILNW MRYTQTVDIW SVGCIMAEMI TGKTLFKGSD HLDQLKEIMK VTGTPPAEFV QRLQSDEAKN YMKGLPELEK KDFASILTNA SPLAVNLLEK MLVLDAEQRV TAGEALAHPY FESLHDTEDE PQVQKYDDSF DDVDRTLDEW KRVTYKEVLS FKPPRQLGAR VSKETPL.

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.

Description:

RELM-Beta Mouse Recombinant

Resistin-like beta, RELM beta, Cysteine-rich secreted protein FIZZ2, Colon and small intestine-specific cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 1, Colon carcinoma-related gene protein, RELM-b, XCP2, HXCP2.

Product # :

CYT-413

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Description

Mouse RELM-b Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 83 amino acids and having a molecular mass of 8.9kDa. The Mouse RETNLB is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) protein solution containing 10mM Acetic Acid with 2:1 mannitol to protein.

Purity

Greater than 97% as determined by SDS-PAGE.

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Introduction
RELM-beta (Resistin-Like Molecule-beta) is a member of a recently identified family of secreted proteins containing a conserved cystein-rich C-terminus. The RELM family consists of resistin (also called FIZZ3), RELM-alfa (FIZZ1), RELM-beta (FIZZ2) and RELM-gamma. Only resisistin and RELM-beta were found in humans whereas all four RELM family members were identified in rodents.
RELM-beta appears to be produced as a homodimer exclusively by intestinal goblet cells and can be found in high quantities in stool. Remarkably, stool of germ-free mice displaying sterile intestinal tract does not contain RELM-beta until bacterial colonization takes place after pathogen-free mice entered natural environment. Some, but not all, colon carcinoma cell lines secrete RELM-beta into the cell culture supernatant.
The physiological function of RELM-beta is not known. High doses of recombinant RELM-beta showed hyperglycemic effects including lowered glucose disposal and increased hepatic glucose production in mice.
Synonyms
Resistin-like beta, RELM beta, Cysteine-rich secreted protein FIZZ2, Colon and small intestine-specific cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 1, Colon carcinoma-related gene protein, RELM-b, XCP2, HXCP2.
Physical Appearance
Brownish lyophilized powder.
Stability
Lyophilized RETNLB is stable at -20°C. After reconstitution the protein should be kept at all times at -20°C. It is recommended to add a carrier protein (0.1% HSA or BSA) for long term storage.
Solubility
Reconstitute at 0.1 mg/ml with sterile pyrogen free water.
Amino Acid Sequence
MQCSFESLVD QRIKEALSRQ EPKTISCTSV TSSGRLASCP AGMVVTGCAC GYGCGSWDIR NGNTCHCQCS VMDWASARCC RMA.

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.

Description:

RELM-Gamma Mouse Recombinant

Resistin-like gamma, RELMgamma,RELM-γ, RELM-g.

Product # :

CYT-1035

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Description

RELM g Mouse Recombinant produced in E.Coli is a non glycosylated, homodimeric polypeptide chain containing 2 x 89 amino acids and having a total molecular mass of 18.9kDa. The RELM is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a sterile filtered solution containing 0.1 % trifluoroacetic acid (TFA).

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
RELM-gamma is a novel member of the resistin-like molecule/found in inflammatory zone (RELM/FIZZ) family in mice and rats. Microarray and real-time RT-PCR experiments revealed a repression of RELMgamma mRNA in nasal respiratory epithelium of cigarette smoke-exposed versus untreated rats. The analysis of the physiological tissue-specific expression revealed highest expression in hematopoietic tissues, suggesting a cytokine-like role for RELM-gamma. RELM-gamma-mRNA is detectable in bone marrow, spleen, and lung as well as in peripheral blood granulocytes. Promyelocytic HL60 cells transfected with a RELM-gamma expression plasmid have an increased proliferation rate compared to mock-transfected cells and display an altered response to retinoic acid-induced granulocytic differentiation. Taken together, these data provide the first experimental evidence that RELM-gamma is a secreted molecule with a restricted expression pattern that may play a role in promyelocytic differentiation.
Synonyms
Resistin-like gamma, RELMgamma,RELM-γ, RELM-g.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized RELM g although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution RELM g Mouse 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.
Solubility
It is recommended to reconstitute the lyophilized RELM g in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MEGTLESIVE KKVKELLANR DDCPSTVTKT FSCTSITASG RLASCPSGMT VTGCACGYGC GSWDIRDGNT CHCQCSTMDW ATARCCQLA.

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.

Description:

Brain-Derived Neurotrophic Factor Human Recombinant, CHO

Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

Product # :

CYT-1262

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Description

Brain-derived Neurotrophic Factor Human Recombinant produced in CHO is a homodimer, polypeptide chain containing 2 x 119 amino acids and having a total molecular mass of 27kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.

Source

CHO Cells

Formulation

The protein was lyophilized with 5% trehalose and 1x PBS

Purity

Greater than 97.0% as determined by SDS-PAGE and SEC-HPLC analyses.

Biological Activity

BDNF CHO activity is determined by its ability to bind recombinant human TrkB Fc Chimera in a functional ELISA assay.

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Introduction
BDNF is crucial for the signal survival eukaryotes. BDNF is responsible for the development, repair, adaptation and proper functionality of the nervous system.
BDNF major roles include Neuron survival and development, synaptic flexibility, stress adaptation, Repair and recovery post injury/disease and Pain signaling.
Synonyms
Brain-Derived Neurotrophic Factor, BDNF, MGC34632.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BDNF 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.
Solubility
It is recommended to reconstitute the lyophilized BDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.
Background
Final Thoughts
Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.
What is the molecular weight/Mw of BDNF Protein?
BDNF Protein has a total Mw of 27kDa.

What is the source or expression system of BDNF Protein?
CHO Cells

What is the Purity of BDNF Protein?
BDNF Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of BDNF Protein?
BDNF CHO activity is determined by its ability to bind recombinant human TrkB Fc Chimera in a functional ELISA assay.

What is the amino acid sequence of BDNF Protein?
HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

What applications can BDNF Protein be used in?
BDNF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BDNF Protein?
The endotoxin level is minimal, BDNF Protein was purified using conventional chromatography techniques.
References
Title:Generation of Neurons with Improved Cell Survival and Phenotype Maintenance Using a Degradation-Resistant Nurr1 Mutant†‡
Publication:Article first published online: 11 JUN 2009 DOI: 10.1002/stem.146 Copyright © 2009 AlphaMed Press.
Link:BDNF prospec publication

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.

Description:

Interleukin-18 Binding Protein Human Recombinant, Sf9

Interleukin 18 Binding Protein, MC51L-53L-54L Homolog Gene Product, Tadekinig-Alfa, IL-18BP, Interleukin-18-Binding Protein, IL18BPa, Interleukin-18-binding protein, IL-18BP, Tadekinig-alfa.

Product # :

CYT-878

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Description

IL18BP Human Recombinant produced in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 406 amino acids (31-194a.a) and having a molecular mass of 44.9kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). IL18BP is fused to a 239 amino acid hIgG-His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL18BP protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Interleukin-18 Binding Protein (IL18BP) serves as an inhibitor of the proinflammatory cytokine, IL18. IL18BP binds IL18, inhibits the binding of IL18 to its receptor, and consequently inhibits IL18-induced IFN-gamma production, resulting in reduced T-helper type 1 immune responses. The IL18BP protein is constitutively expressed and secreted in mononuclear cells. Elevated levels of IL18BP protein are detected in the intestinal tissues of patients with Crohn's disease.
Synonyms
Interleukin 18 Binding Protein, MC51L-53L-54L Homolog Gene Product, Tadekinig-Alfa, IL-18BP, Interleukin-18-Binding Protein, IL18BPa, Interleukin-18-binding protein, IL-18BP, Tadekinig-alfa.
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
ADPTPVSQTT TAATASVRST KDPCPSQPPV FPAAKQCPAL EVTWPEVEVP LNGTLSLSCV ACSRFPNFSI LYWLGNGSFI EHLPGRLWEG STSRERGSTG TQLCKALVLE QLTPALHSTN FSCVLVDPEQ VVQRHVVLAQ LWAGLRATLP PTQEALPSSH SSPQQQGLEP 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.

Description:

Vascular Endothelial Growth Factor receptor-1 Mouse Recombinant

FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

Product # :

PKA-139

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Description

FLT1 Mouse Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (23-759 a.a) containing a total of 970 amino acids, having a molecular mass of 108.9kDa. FLT1 is fused to a 233 amino acid hIgG-his tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK 293.

Formulation

FLT1 protein solution (1mg/ml) containing 10% glycerol and PBS.

Purity

Greater than 85.0% as determined by SDS-PAGE.

Biological Activity

The ED50 range ≤ 50ng/ml and is measured by its ability to inhibit proliferation using HUVEC human umbilical vein endothelial cells in the presence of Human VEGF165.

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Synonyms
FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
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
YGSGSKLKVP ELSLKGTQHV MQAGQTLFLK CRGEAAHSWS LPTTVSQEDK RLSITPPSAC GRDNRQFCST LTLDTAQANH TGLYTCRYLP TSTSKKKKAE SSIYIFVSDA GSPFIEMHTD IPKLVHMTEG RQLIIPCRVT SPNVTVTLKK FPFDTLTPDG QRITWDSRRG FIIANATYKE IGLLNCEATV NGHLYQTNYL THRQTNTILD VQIRPPSPVR LLHGQTLVLN CTATTELNTR VQMSWNYPGK ATKRASIRQR IDRSHSHNNV FHSVLKINNV ESRDKGLYTC RVKSGSSFQS FNTSVHVYEK GFISVKHRKQ PVQETTAGRR SYRLSMKVKA FPSPEIVWLK DGSPATLKSA RYLVHGYSLI IKDVTTEDAG DYTILLGIKQ SRLFKNLTAT LIVNVKPQIY EKSVSSLPSP PLYPLGSRQV LTCTVYGIPR PTITWLWHPC HHNHSKERYD FCTENEESFI LDPSSNLGNR IESISQRMTV IEGTNKTVST LVVADSQTPG IYSCRAFNKI GTVERNIKFY VTDVPNGFHV SLEKMPAEGE DLKLSCVVNK FLYRDITWIL LRTVNNRTMH HSISKQKMAT TQDYSITLNL VIKNVSLEDS GTYACRARNI YTGEDILRKT EVLVRDSEAP HLLQNLSDYE VSISGSTTLD CQARGVPAPQ ITWFKNNHKI QQEPGIILGP GNSTLFIERV TEEDEGVYRC RATNQKGAVE
Background
Endothelial cells express 3 different vascular endothelial growth factor receptors: VEGFR-1 (Flt1), VEGFR-2 (KDR/Flk1), VEGFR-3 (Flt4) which are a part of the receptor tyrosine kinases family. Those receptors express mostly in endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. Flt1 contains 7 immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Flt-1, when compared to VEGFR-2 receptor has a higher affinity for VEGF but a weaker signalling activity. VEGFR-1 also mediates signals for differentiation.

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.

Description:

Melanoma Antigen Family A, 3 Human Recombinant

CT1.3, MAGE3, HYPD, Melanoma Antigen family A, 3, MAGE-3 antigen, MAGEA6, Antigen MZ2-D, Melanoma-Associated antigen 3.

Product # :

PRO-502

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Description

MAGEA3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 337 amino acids (1-314 a.a.) and having a molecular mass of 37.1kDa.MAGEA3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MAGEA3 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) 1mM DTT, 100mM NaCl and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
MAGE belongs to the MAGE gene family, that comprises 12 known genes, of which 6 are expressed in tumors. The Melanoma-associated antigen 3 genes were originally isolated from different kinds of tumors, and based on their virtually limited tumor-specific expression in adult tissues, they were used as targets for cancer immunotherapy. MAGEA3 is a tumor-specific antigen extensively expressed in solid and hematologic malignancies, but not in normal tissues, with the exclusion of testis and placenta. Consequently, MAGEA3 is an outstanding candidate tumor antigen.
Synonyms
CT1.3, MAGE3, HYPD, Melanoma Antigen family A, 3, MAGE-3 antigen, MAGEA6, Antigen MZ2-D, Melanoma-Associated antigen 3.
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 MGSMPLEQRS QHCKPEEGLE ARGEALGLVG AQAPATEEQE AASSSSTLVE VTLGEVPAAE SPDPPQSPQG ASSLPTTMNY PLWSQSYEDS SNQEEEGPST FPDLESEFQA ALSRKVAELV HFLLLKYRAR EPVTKAEMLG SVVGNWQYFF PVIFSKASSS LQLVFGIELM EVDPIGHLYI FATCLGLSYD GLLGDNQIMP KAGLLIIVLA IIAREGDCAP EEKIWEELSV LEVFEGREDS ILGDPKKLLT QHFVQENYLE YRQVPGSDPA CYEFLWGPRA LVETSYVKVL HHMVKISGGP HISYPPLHEW VLREGEE

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Interleukin-6 Mouse Recombinant, Sf9

Interleukin-6, IL-6, B-cell hybridoma growth factor, Interleukin HP-1.

Product # :

CYT-904

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Description

Interleukin-6 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 193 amino acids (25-211a.a.) and having a molecular mass of 22.5kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). IL6 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL 6 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

Measured in a cell proliferation assay using M-NFS-60 mouse B cell. The ED₅₀ for this effect is less or equal to 0.1 ng/ml.

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Introduction
Il-6 is a cytokine with a wide variety of biological functions: it plays an essential role in the final differentiation of b-cells into ig-secreting cells, it induces myeloma and plasmacytoma growth, it induces nerve cells differentiation, in hepatocytes it induces acute phase reactants.
Synonyms
Interleukin-6, IL-6, B-cell hybridoma growth factor, Interleukin HP-1.
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
FPTSQVRRGD FTEDTTPNRP VYTTSQVGGL ITHVLWEIVE MRKELCNGNS DCMNNDDALA ENNLKLPEIQ RNDGCYQTGY NQEICLLKIS SGLLEYHSYL EYMKNNLKDN KKDKARVLQR DTETLIHIFN QEVKDLHKIV LPTPISNALL TDKLESQKEW LRTKTIQFIL KSLEEFLKVT LRSTRQTHHH HHH.
Background
Research Paper on Interleukin-6 Mouse Recombinant, Sf9
Abstract:
Exploring Interleukin-6 Mouse Recombinant, Sf9, a fascinating research topic! This paper provides an extensive description of Interleukin-6 (IL-6) Mouse Recombinant expressed in Sf9 insect cells. We delve into the molecular properties of IL-6, its significance in immune responses and inflammation, and its synonyms, including DIF, TNFA, and TNFSF2. Join us as we uncover the potential applications of IL-6 research using this novel recombinant mouse protein.
Introduction:
Introducing Interleukin-6 Mouse Recombinant, Sf9. This paper sheds light on the production and characteristics of IL-6 expressed in Sf9 insect cells. As researchers, we are intrigued by the versatility and applications of this recombinant protein in immunological studies.
An Extensive Description of Interleukin-6 Mouse Recombinant:
We present a comprehensive overview of Interleukin-6 Mouse Recombinant, focusing on its structure and functions. This recombinant protein enables us to explore IL-6's role in various cellular processes, making it a valuable tool for investigating immune regulation.
Significance in Immune Responses:
Marvel at IL-6's critical role in orchestrating immune responses! As a key cytokine, IL-6 plays a central role in immune cell activation and the regulation of inflammatory processes. Its pleiotropic effects contribute to maintaining homeostasis in the immune system.
Interactions and Synonyms:
Learn about the synonyms associated with IL-6, such as DIF, TNFA, and TNFSF2. Understanding these synonyms enhances our understanding of the interconnectedness of cytokine signaling. The complex interactions between IL-6 and other molecules further enrich our knowledge of immune responses.
Potential Applications in Immunological Research:
Explore the wide range of applications of Interleukin-6 Mouse Recombinant in immunological studies. From cell-based assays to therapeutic developments, this recombinant protein offers novel avenues for advancing immunology research. It serves as a valuable tool in deciphering the intricate immune system functions.
Novel Production Method using Sf9 Insect Cells:
Discover the innovative use of Sf9 insect cells for producing Interleukin-6. This expression system provides a scalable and efficient approach for obtaining large quantities of functional IL-6. The use of Sf9 cells opens up possibilities for large-scale protein production and downstream applications.
Conclusion:
Concluding our exploration of Interleukin-6 Mouse Recombinant, Sf9, we recognize its significance in immunological research. The extensive description of this recombinant protein broadens our understanding of IL-6 biology and its potential applications in various fields. As researchers, we are excited about the potential discoveries that lie ahead with the help of this valuable tool.

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.

Description:

CD300A Human Recombinant

CD300a Molecule, CD300a Antigen, IRp60, CD300 Antigen-Like Family Member A, NK Inhibitory Receptor, Immunoglobulin Superfamily Member 12, CMRF35-Like Molecule 8, CMRF35-H, Inhibitory Receptor Protein 60, CMRF-35-H9, CMRF-35H, CLM-8, IRC1, IRC2, CMRF35H Leukocyte Immunoglobulin-Like Receptor, Leukocyte Membrane Antigen, IgSF12.

Product # :

PRO-1618

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Description

CD300A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 134 amino acids (18-128) and having a molecular mass of 14.7kDa.CD300A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CD300A solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
CD300A belongs to the CD300 family and contains 1 Ig-like V-type (immunoglobulin-like) domain. The protein is expressed not only by natural killer (NK) cells but also by T-cell subsets, B-cells, dendritic cells, mast cells, granulocytes and monocytes. CD300A is inhibitory receptor which may contribute to the down-regulation of cytolytic activity in natural killer (NK) cells, and to the down-regulation of mast cell degranulation.
Synonyms
CD300a Molecule, CD300a Antigen, IRp60, CD300 Antigen-Like Family Member A, NK Inhibitory Receptor, Immunoglobulin Superfamily Member 12, CMRF35-Like Molecule 8, CMRF35-H, Inhibitory Receptor Protein 60, CMRF-35-H9, CMRF-35H, CLM-8, IRC1, IRC2, CMRF35H Leukocyte Immunoglobulin-Like Receptor, Leukocyte Membrane Antigen, IgSF12.
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 MGSLSKCRTV AGPVGGSLSV QCPYEKEHRT LNKYWCRPPQ IFLCDKIVET KGSAGKRNGR VSIRDSPANL SFTVTLENLT EEDAGTYWCG VDTPWLRDFH DPVVEVEVSV FPAS

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.

Description:

Cytotoxic T-Lymphocyte Associated Antigen-4 Human Recombinant

GSE, CD152, IDDM12, CELIAC3, CTLA-4.

Product # :

CYT-366

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sds-page

Description

CTLA 4 Human Recombinant produced in E. coli is a single polypeptide chain containing 149 amino acids (36-161) and having a molecular mass of 15.9 kDa.CTLA 4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CTLA 4 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
CTLA-4 is a member of the immunoglobulin superfamily and encodes a protein which transmits an inhibitory signal to T cells. The protein contains a V domain, a transmembrane domain, and a cytoplasmic tail. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. The membrane-bound isoform functions as a homodimer interconnected by a disulfide bond, while the soluble isoform functions as a monomer. Mutations in this gene have been associated with insulin-dependent diabetes mellitus, Graves disease, Hashimoto thyroiditis, celiac disease, systemic lupus erythematosus, thyroid-associated orbitopathy, and other autoimmune diseases.
Synonyms
GSE, CD152, IDDM12, CELIAC3, CTLA-4.
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 MGSKAMHVAQ PAVVLASSRG IASFVCEYAS PGKATEVRVT VLRQADSQVT EVCAATYMMG NELTFLDDSI CTGTSSGNQV NLTIQGLRAM DTGLYICKVE LMYPPPYYLG IGNGTQIYVI DPEPCPDSD.
Background
Title: Cytotoxic T-Lymphocyte Associated Antigen-4 Human Recombinant: A Potential Immunotherapeutic Target
Abstract:

Cytotoxic T-lymphocyte associated antigen-4 (CTLA-4) is a key immune checkpoint receptor that plays a crucial role in regulating T-cell responses. This research paper provides an in-depth analysis of human recombinant CTLA-4, focusing on its production, characterization, and potential applications in immunotherapy. The paper discusses the significance of CTLA-4 in immune regulation, tumor immunity, and autoimmune diseases. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant CTLA-4 in various pathological conditions. The information presented in this paper aims to enhance our understanding of human recombinant CTLA-4 and its utility as a research tool and a potential immunotherapeutic agent.
Introduction:

Cytotoxic T-lymphocyte associated antigen-4 (CTLA-4) is a cell surface receptor primarily expressed on T-cells. It functions as a negative regulator of T-cell activation, dampening immune responses to prevent excessive inflammation. Human recombinant CTLA-4, produced through genetic engineering techniques, provides researchers with a valuable tool to study its biological functions and explore its therapeutic potential.
Production and Characterization:

Recombinant CTLA-4 is typically generated using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Quality control measures are implemented to confirm the specificity and bioactivity of the recombinant CTLA-4.
Role in Immune Regulation:

CTLA-4 plays a critical role in immune regulation by downregulating T-cell activation and suppressing immune responses. It competes with the co-stimulatory receptor CD28 for binding to its ligands, CD80 and CD86, on antigen-presenting cells. This interaction inhibits T-cell activation and promotes immune tolerance. Recombinant CTLA-4 serves as a valuable tool for studying immune checkpoint mechanisms and their impact on immune responses.
Therapeutic Implications:

The blockade of CTLA-4 has emerged as a promising immunotherapeutic strategy in cancer treatment. Monoclonal antibodies targeting CTLA-4, such as ipilimumab, have shown significant clinical efficacy in enhancing anti-tumor immune responses. Recombinant CTLA-4-based therapies, including fusion proteins and engineered T-cell receptors, are being explored as potential immunotherapeutic interventions. Additionally, CTLA-4 plays a role in autoimmune diseases, making it a potential target for the development of novel treatments.
Conclusion:

Human recombinant CTLA-4 is a valuable research tool and a potential immunotherapeutic target. Its production, characterization, and applications in immune regulation contribute to our understanding of T-cell biology and the development of novel immunotherapies. Continued research and clinical trials investigating the therapeutic potential of recombinant CTLA-4 offer promising prospects for improving outcomes in cancer and autoimmune diseases.
What is the molecular weight/Mw of CTLA4 Protein?
CTLA4 Protein has a total Mw of 15.9kDa.

What is the source or expression system of CTLA4 Protein?
Escherichia Coli.

What is the Purity of CTLA4 Protein?
CTLA4 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of CTLA4 Protein?
The biological functionality of CTLA4 Protein will be determined in the future.

What is the amino acid sequence of CTLA4 Protein?
MGSSHHHHHH SSGLVPRGSH MGSKAMHVAQ PAVVLASSRG IASFVCEYAS PGKATEVRVT VLRQADSQVT EVCAATYMMG NELTFLDDSI CTGTSSGNQV NLTIQGLRAM DTGLYICKVE LMYPPPYYLG IGNGTQIYVI DPEPCPDSD.

What applications can CTLA4 Protein be used in?
CTLA4 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CTLA4 Protein?
The endotoxin level is minimal, CTLA4 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.

Description:

Platelet Factor-4 Mouse Recombinant (CXCL4)

CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.

Product # :

CHM-245

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Description

CXCL4 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 76 amino acids and having a molecular mass of 8.2kDa.

Source

Escherichia Coli.

Formulation

The Mouse CXCL4 protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 7.4 and 1.5M 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 neutrophils using a concentration range of 10-100ng/ml.

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Introduction
Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets. Its major physiologic role appears to be neutralization of molecules on the endothelial surface of blood vessels, thereby inhibiting local activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemocinfamily.
Synonyms
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
Physical Appearance
Sterile Filtered white lyophilized powder.
Stability
Lyophilized CXCL4 Mouse Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Mouse CXCL4 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.
Solubility
It is recommended to reconstitute the lyophilized CXCL4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VTSAGPEESD GDLSCVCVKT ISSGIHLKHI TSLEVIKAGR HCAVPQLIAT LKNGRKICLD RQAPLYKKVI KKILES.

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.

Description:

Cerebral Dopamine Neurotrophic Factor Mouse Recombinant

Cerebral dopamine neurotrophic factor, ARMET-like protein 1, Conserved dopamine neurotrophic factor, Cdnf, Armetl1, 9330140G23.

Product # :

CYT-729

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Description

CDNF Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 163 amino acids and having a molecular mass of 18.5kDa.The CDNF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CDNF protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

CDNF Mouse is able to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons when immobilized at 5-30 µg/mL on a nitrocellulose-coated microplate.

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Introduction
CDNF is a member of the ARMET family and acts as a trophic factor for dopamine neurons. CDNF inhibits the 6-hydroxydopamine (6-OHDA)-induced degeneration of dopaminergic neurons. When CDNF controlled after 6-OHDA-lesioning, it reestablishes the dopaminergic function and inhibits the degeneration of dopaminergic neurons in substantia nigra. CDNF is universally expressed in neuronal and non-neuronal tissues. The highest levels in the brain are found in the optic nerve and corpus callosum.
Synonyms
Cerebral dopamine neurotrophic factor, ARMET-like protein 1, Conserved dopamine neurotrophic factor, Cdnf, Armetl1, 9330140G23.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CDNF 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.
Solubility
It is recommended to reconstitute the lyophilized CDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QGLEAGVGPR ADCEVCKEFL DRFYNSLLSR GIDFSADTIE KELLNFCSDA KGKENRLCYY LGATTDAATK ILGEVTRPMS VHIPAVKICE KLKKMDSQIC ELKYGKKLDL ASVDLWKMRV AELKQILQRW GEECRACAEK SDYVNLIREL APKYVEIYPQ TEL.
Background
What is the molecular weight/Mw of CDNF Protein?
CDNF Protein has a total Mw of 18.5kDa.

What is the source or expression system of CDNF Protein?
Escherichia Coli.

What is the Purity of CDNF Protein?
CDNF Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CDNF Protein?
CDNF Mouse is able to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons when immobilized at 5-30 µg/mL on a nitrocellulose-coated microplate.

What is the amino acid sequence of CDNF Protein?
QGLEAGVGPR ADCEVCKEFL DRFYNSLLSR GIDFSADTIE KELLNFCSDA KGKENRLCYY LGATTDAATK ILGEVTRPMS VHIPAVKICE KLKKMDSQIC ELKYGKKLDL ASVDLWKMRV AELKQILQRW GEECRACAEK SDYVNLIREL APKYVEIYPQ TEL.

What applications can CDNF Protein be used in?
CDNF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CDNF Protein?
The endotoxin level is minimal, CDNF 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.

Description:

Insulin-Like Growth Factor Binding Protein-5 Human Recombinant

IGFBP-5, IBP-5, IGF-binding protein 5.

Product # :

CYT-464

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Description

IGFBP5 Human Recombinant produced in E.Coli is non-glycosylated homodimer containing 2x252 amino acids and having a molecular mass of 28.6kDa. IGFBP5 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IBP-5 was lyophilized from a concentrated (1mg/ml) solution containing 10mM sodium Citrate pH-3.

Purity

Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀, calculated by its ability to inhibit IGF-II induced proliferation of MCF-7. The expected ED50 for this effect is < 0.4µg/ml, corresponding to a specific activity of > 2500 IU/mg in the presence of 15ng/ml of rHuIGF-II.

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Introduction
IGFBP5 is a member of the insulin-like growth factor binding protein (IGFBP) family and encodes a protein with an IGFBP domain and a thyroglobulin type-I domain. The protein forms a ternary complex with insulin-like growth factor acid-labile subunit (IGFALS) and either insulin-like growth factor (IGF) I or II. In this form, it circulates in the plasma, prolonging the half-life of IGFs and altering their interaction with cell surface receptors. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
Synonyms
IGFBP-5, IBP-5, IGF-binding protein 5.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IBP5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGFBP 5 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.
Solubility
It is recommended to reconstitute the lyophilized Insulin-Like Growth Factor Binding Protein-5 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
LGSFVHCEPC DEKALSMCPP SPLGCELVKE PGCGCCMTCA LAEGQSCGVY TERCAQGLRC LPRQDEEKPL HALLHGRGVC LNEKSYREQV KIERDSREHE EPTTSEMAEE TYSPKIFRPK HTRISELKAE AVKKDRRKKL TQSKFVGGAE NTAHPRIISA PEMRQESEQG PCRRHMEASL QELKASPRMV PRAVYLPNCD RKGFYKRKQC KPSRGRKRGI CWCVDKYGMK LPGMEYVDGD FQCHTFDSSN VE.

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.

Description:

Platelet Derived Growth Factor-D Human Recombinant

Platelet Derived Growth Factor D, Spinal Cord-Derived Growth Factor B, Iris-Expressed Growth Factor, SCDGF-B, IEGF, PDGF-D, MSTP036.

Product # :

CYT-155

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Description

PDGFD Human Recombinant produced in E. coli is a single polypeptide chain containing 146 amino acids (250-370) and having a molecular mass of 16.6 kDa.PDGFD is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The PDGFD solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Platelet-derived growth factor D (PDGFD) belongs to the platelet-derived growth factor family. PDGFD gene product only forms homodimers and, thus, does not dimerize with the other 3 family members. PDGFD has an imperative role in wound healing. PDGFD induces macrophage recruitment, increased interstitial pressure, and blood vessel maturation during angiogenesis. PDGFD initiates events which lead to a mesangial proliferative glomerulonephritis, including influx of monocytes and macrophages and production of extracellular matrix. The 4 members of the PDGF family are mitogenic factors for cells of mesenchymal origin and are distinguished by a core motif of eight cysteines, 7 of which are found in this factor. PDGFD differs from alpha and beta members of this family by having an odd N-terminal domain, the CUB domain.
Synonyms
Platelet Derived Growth Factor D, Spinal Cord-Derived Growth Factor B, Iris-Expressed Growth Factor, SCDGF-B, IEGF, PDGF-D, MSTP036.
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 MGSHMSYHDR KSKVDLDRLN DDAKRYSCTP RNYSVNIREE LKLANVVFFP RCLLVQRCGG NCGCGTVNWR SCTCNSGKTV KKYHEVLQFE PGHIKRRGRA KTMALVDIQL DHHERCDCIC SSRPPR.

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.

Description:

Leptin Human Recombinant, PEG

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-1108

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Description

Pegylated Leptin Human Recombinant produced in E.Coli is a single non-glycosilated polypeptide chain containing 146 amino acids, an additional Ala at N-terminus and one molecule of PEG 20 kDa at its N-terminus acids and having a molecular weight of 35.6kDa. 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 100 kDa protein. Pegylated Leptin Human Recombinant was purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

Purity

Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.

Biological Activity

Biological Activity is < than 0.1% as determined by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It’s in vitro activity is 5-7 fold lower than the non-pegylated recombinant human leptin but in vivo it has profound weight reducing effect, resulting mainly from reduced food intake.

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Introduction
Leptin takes an important part in the regulation of energy balance and body weight control.After entering the circulation, Leptin binds LEPRwhich results in the activation of several major signalling pathways. In the hypothalamus Leptin acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption and also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, regulates pancreatic beta-cell function and insulin secretion and affects innate and adaptive immunity.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Pegylated leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution leptin N82K 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.
Solubility
It is recommended to reconstitute the lyophilized Pegylated leptin 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.
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.87 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.

Description:

Calcium/Calmodulin-Dependent Protein Kinase II Inhibitor 2 Human Recombinant

Calcium/calmodulin-dependent protein kinase II inhibitor 2, CAMK2N2, CaM-KII inhibitory protein, CaM-KIIN, CAMKIIN, Calcium/calmodulin-dependent protein kinase II.

Product # :

PKA-311

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Description

CAMK2N2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 102 amino acids (1-79a.a) and having a molecular mass of 11kDa.CAMK2N2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

CAMK2N2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Calcium/Calmodulin-Dependent Protein Kinase II Inhibitor 2 (CAMK2N2) is a protein coding gene which regulates cell growth when overexpressed in colon adenocarcinoma LoVo cells. CAMK2N2 plays a role as a cellular inhibitor of CaM-kinase II (CAMK2).
Synonyms
Calcium/calmodulin-dependent protein kinase II inhibitor 2, CAMK2N2, CaM-KII inhibitory protein, CaM-KIIN, CAMKIIN, Calcium/calmodulin-dependent protein kinase II.
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 MGSMSEILPY SEDKMGRFGA DPEGSDLSFS CRLQDTNSFF AGNQAKRPPK LGQIGRAKRV VIEDDRIDDV LKGMGEKPPS GV.

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.

Description:

TNF Ligand Receptor Superfamily Member 25 Recombinant Human

Tumor necrosis factor receptor superfamily member 25, TNFRSF25, TNF Ligand Receptor Superfamily Member 25, APO-3, DDR3, DR3, LARD, TNFRSF12, TR3, TRAMP, WSL-1, WSL-LR, Apo-3, Apoptosis-inducing receptor AIR, Protein WSL, Apoptosis-mediating receptor DR3, Apoptosis-mediating receptor TRAMP, Death receptor 3, Lymphocyte-associated receptor of death.

Product # :

CYT-980

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Description

TNFRSF25 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 417 amino acids (25-199) and having a molecular mass of 46.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). TNFRSF25 is fused to a 242 amino acid IgG His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

TNFRSF25 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by analysis by SDS-PAGE.

Biological Activity

Determined by the binding ability in a functional ELISA with Human VEGI (CAT# cyt-589). The ED50 range ≤ 5ug/ml.

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Introduction
TNF Ligand Receptor Superfamily Member 25 (TNFRSF25) belongs to the TNF receptor superfamily that binds to the TNF-like protein TL1A. TNFRSF25 interacts directly with the adapter TRADD and regulates lymphocyte homeostasis. TNFRSF25 is also mediates activation of NF-kappa-B and induces apoptosis. TNFRSF25 signals are vital to exert T helper cell 2 effector activity in Th2-polarized CD4 cells and co-stimulate interleukin-13 production by glycosphingolipid-activated NKT cells.
Synonyms
Tumor necrosis factor receptor superfamily member 25, TNFRSF25, TNF Ligand Receptor Superfamily Member 25, APO-3, DDR3, DR3, LARD, TNFRSF12, TR3, TRAMP, WSL-1, WSL-LR, Apo-3, Apoptosis-inducing receptor AIR, Protein WSL, Apoptosis-mediating receptor DR3, Apoptosis-mediating receptor TRAMP, Death receptor 3, Lymphocyte-associated receptor of death.
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
ADPQGGTRSP RCDCAGDFHK KIGLFCCRGC PAGHYLKAPC TEPCGNSTCL VCPQDTFLAW ENHHNSECAR CQACDEQASQ VALENCSAVA DTRCGCKPGW FVECQVSQCV SSSPFYCQPC LDCGALHRHT RLLCSRRDTD CGTCLPGFYE HGDGCVSCPT STLGSCPERC AAVCGWRQLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.

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.

Description:

Peroxisomal Biogenesis Factor 19 Human Recombinant

Peroxisomal biogenesis factor 19, Peroxisomal farnesylated protein, HK33, 33kDa housekeeping protein, PXF, PMP1, PXMP1, Peroxin-19, D1S2223E, FLJ55296.

Product # :

PRO-925

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Description

PEX19 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 316 amino acids (1-296) and having a molecular mass of 34.6 kDa.The PEX19 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The PEX19 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
PEX19 is vital for peroxisome biogenesis in Saccharomyces cerevisiae. PEX19 is limited to the outer surface of peroxisomes in liver cells and is has a part in the early stage of peroxisome membrane assembly, prior to the import of matrix protein.
Synonyms
Peroxisomal biogenesis factor 19, Peroxisomal farnesylated protein, HK33, 33kDa housekeeping protein, PXF, PMP1, PXMP1, Peroxin-19, D1S2223E, FLJ55296.
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 MAAAEEGCSV GAEADRELEE LLESALDDFD KAKPSPAPPS TTTAPDASGP QKRSPGDTAK DALFASQEKF FQELFDSELA SQATAEFEKA MKELAEEEPH LVEQFQKLSE AAGRVGSDMT SQQEFTSCLK ETLSGLAKNA TDLQNSSMSE EELTKAMEGL GMDEGDGEGN ILPIMQSIMQ NLLSKDVLYP SLKEITEKYP EWLQSHRESL PPEQFEKYQE QHSVMCKICE QFEAETPTDS ETTQKARFEM VLDLMQQLQD LGHPPKELAG EMPPGLNFDL DALNLSGPPG ASGEQC

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.

Description:

Cell Adhesion Molecule 1 Human Recombinant

Cell Adhesion Molecule 1, Tumor Suppressor In Lung Cancer 1, IGSF4, Spermatogenic Immunoglobulin Superfamily, Immunoglobulin Superfamily, Member 4, Immunoglobulin Superfamily Member 4, Synaptic Cell Adhesion Molecule, Nectin-Like Protein 2, Nectin-Like 2, Necl-2, SgIGSF, IGSF4A, SYNCAM, TSLC-1, TSLC1, NECL2, Immunoglobulin Superfamily, Member 4D Variant 1, Immunoglobulin Superfamily, Member 4D Variant 2, TSLC1/Nectin-Like 2/IGSF4, Truncated CADM1 Protein, STSLC-1, SynCAM1, RA175, ST17, BL2, Cell adhesion molecule 1.

Product # :

PRO-2098

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Description

CADM1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 353 amino acids (45-374 a.a) and having a molecular mass of 39.4 kDa. CADM1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CADM1 protein solution (0.25 mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Cell Adhesion Molecule 1, also known as CADM1 belongs to the nectin family. CADM1 mediates homophilic cell-cell adhesion in a Ca2+-independent manner as well as mediating heterophilic cell-cell adhesion with CADM3 and PVRL3 in a Ca2+-independent manner. Furthermore, CADM1 perform as a tumor suppressor in non-small-cell lung cancer, NSCLC, cells. The interaction with CRTAM promotes natural killer (NK) cell cytotoxicity & IFN-gamma secretion by CD8+ cells in vitro over and above NK cell-mediated rejection of tumors expressing CADM3 in vivo.
Synonyms
Cell Adhesion Molecule 1, Tumor Suppressor In Lung Cancer 1, IGSF4, Spermatogenic Immunoglobulin Superfamily, Immunoglobulin Superfamily, Member 4, Immunoglobulin Superfamily Member 4, Synaptic Cell Adhesion Molecule, Nectin-Like Protein 2, Nectin-Like 2, Necl-2, SgIGSF, IGSF4A, SYNCAM, TSLC-1, TSLC1, NECL2, Immunoglobulin Superfamily, Member 4D Variant 1, Immunoglobulin Superfamily, Member 4D Variant 2, TSLC1/Nectin-Like 2/IGSF4, Truncated CADM1 Protein, STSLC-1, SynCAM1, RA175, ST17, BL2, Cell adhesion molecule 1.
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 MGSQNLFTKD VTVIEGEVAT ISCQVNKSDD SVIQLLNPNR QTIYFRDFRP LKDSRFQLLN FSSSELKVSL TNVSISDEGR YFCQLYTDPP QESYTTITVL VPPRNLMIDI QKDTAVEGEE IEVNCTAMAS KPATTIRWFK GNTELKGKSE VEEWSDMYTV TSQLMLKVHK EDDGVPVICQ VEHPAVTGNL QTQRYLEVQY KPQVHIQMTY PLQGLTREGD ALELTCEAIG KPQPVMVTWV RVDDEMPQHA VLSGPNLFIN NLNKTDNGTY RCEASNIVGK AHSDYMLYVY DPPTTIPPPT TTTTTTTTTT TTILTIITDS RAGEEGSIRA VDH.

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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