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Name :
GAL HumanDescription:
Galanin Prepropeptide Human Recombinant
GALN, GLNN, GMAP, GAL, GAL1.
Product # :
PRO-1433Price :
Quantity :
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Shipped with Ice Packs
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Description
GAL Human Recombinant produced in E. coli is a single polypeptide chain containing 127 amino acids (20-123) and having a molecular mass of 13.9kDa. GAL is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GAL solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Galanin Prepropeptide (GAL) which is localized in brain pathways is involved in both cognition and affect, and also inhibits learning and memory by inhibiting neurotransmitter release and neuronal firing rate. GAL is a part of the galanin family and modulates a variety of physiological processed including cognition/memory, sensory/pain processing, neurotransmitter/hormone secretion, and feeding behavior. Galanin Prepropeptide is upregulated in primary afferent and sympathetic neurones and is required for the development of sympathetic perineuronal baskets subsequent to nerve injury.
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Synonyms
GALN, GLNN, GMAP, GAL, GAL1.
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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 MGSASAGLWS PAKEKRGWTL NSAGYLLGPH AVGNHRSFSD KNGLTSKREL RPEDDMKPGS FDRSIPENNI MRTIIEFLSF LHLKEAGALD RLLDLPAAASSEDIERS.
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 :
KLK11 Human, Sf9Description:
Kallikrein-11, 4 Human Recombinant, Sf9
Kallikrein-11 isoform 1, KLK11, PRSS20, TLSP.
Product # :
ENZ-1089Price :
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Description
KLK11 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 241 amino acids (19-250a.a.) and having a molecular mass of 26.7 kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).KLK11 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
KLK11 protein solution ( 0.5mg/m ) contains 50mM Tris-HCl (pH 7.5), 0.1M NaCl, 2mM CaCl2 and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Kallikreins are a subgroup of serine proteases having various physiological functions. Numerous kallikreins are involved in carcinogenesis. Kallikrein-11 (KLK11) which is a multifunctional protease is 1 of the 15 kallikrein subfamily members found in a cluster on chromosome 19. KLK11 cleaves synthetic peptides after arginine but not lysine residues.
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Synonyms
Kallikrein-11 isoform 1, KLK11, PRSS20, TLSP.
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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
ADLETRIIKG FECKPHSQPW QAALFEKTRL LCGATLIAPR WLLTAAHCLK PRYIVHLGQH NLQKEEGCEQ TRTATESFPH PGFNNSLPNK DHRNDIMLVK MASPVSITWA VRPLTLSSRC VTAGTSCLIS GWGSTSSPQL RLPHTLRCAN ITIIEHQKCE NAYPGNITDT MVCASVQEGG KDSCQGDSGG PLVCNQSLQG IISWGQDPCA ITRKPGVYTK VCKYVDWIQE TMKNNHHHHH H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CCL15 HumanDescription:
Macrophage Inflammatory Protein-5 Human Recombinant (CCL15)
Small inducible cytokine A15 precursor, CCL15, Macrophage inflammatory protein 5, MIP-5, MIP5, Chemokine CC-2, HCC-2, NCC-3, MIP- 1 delta, Leukotactin-1, LKN-1, Mrp-2b, C-C motif chemokine 15.
Product # :
CHM-230Price :
Quantity :
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Shipped at Room temp
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Description
Macrophage Inflammatory Protein-5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 92 amino acids and having a molecular mass of 10.1 kDa. The MIP5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MIP5 was lyophilized from a concentrated (1mg/ml) solution containing 20mM PBS pH-7.4 and 100mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human T-lymphocytes using a concentration range of 1-10 ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.More Info
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Introduction
CCL15, a new human CC chemokine, was isolated from a human fetal spleen cDNA library. CCL15 cDNA encodes a predicted 113 amino acid (aa) protein containing a putative signal peptide of 21 amino acids that is cleaved to generate a 92 aa residue mature protein. Within the CC family members, human CCL15 shares 45%, 44%, 35%, and 30% aa homology with mouse C10, human MPIF-1, human HCC-1, and mouse MIP-1?, respectively. The gene for MIP-5 is found on chromosome 17 where the genes for most of the human CC chemokines are located. Human CCL15 is expressed in T and B lymphocytes, NK cells, monocytes and monocyte-derived dendritic cells. Human MIP-5 is chemotactic for T cells and monocytes and has been shown to induce calcium flux in human CCR-1-transfected cells.
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Synonyms
Small inducible cytokine A15 precursor, CCL15, Macrophage inflammatory protein 5, MIP-5, MIP5, Chemokine CC-2, HCC-2, NCC-3, MIP- 1 delta, Leukotactin-1, LKN-1, Mrp-2b, C-C motif chemokine 15.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MIP-5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL15 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 MIP5 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
QFINDAETELMMSKLPLENPVVLNSFHFAADCCTSYISQSIPCSLMKSYFETSSECSKP GVIFLTKKGRQVCAKPSGPGVQDCMKKLKPYSI.
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Background
What is the molecular weight/Mw of CCL15 HUMAN Protein?
CCL15 HUMAN Protein has a total Mw of 10.1kDa.
What is the source or expression system of CCL15 HUMAN Protein?
Escherichia Coli.
What is the Purity of CCL15 HUMAN Protein?
CCL15 HUMAN Protein is > 97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL15 HUMAN Protein?
Determined by its ability to chemoattract human T-lymphocytes using a concentration range of 1-10 ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.
What is the amino acid sequence of CCL15 HUMAN Protein?
QFINDAETELMMSKLPLENPVVLNSFHFAADCCTSYISQSIPCSLMKSYFETSSECSKP GVIFLTKKGRQVCAKPSGPGVQDCMKKLKPYSI.
What applications can CCL15 HUMAN Protein be used in?
CCL15 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL15 HUMAN Protein?
The endotoxin level is minimal, CCL15 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 :
Enterokinase BovineDescription:
Enteropeptidase/ Enterokinase Light Chain Bovine Recombinant
Enteropeptidase, EC 3.4.21.9, Enterokinase, Serine protease 7, ENTK, MGC133046.
Product # :
ENZ-311Price :
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Description
Enterokinase (rEK) Bovine Recombinant is the catalytic subunit of bovine enterokinase, which is expressed by E. Coli and purified to yield a high enzyme activity preparation. EK recognizes the sequence Asp-Asp-Asp-Asp-Lys and cleaves the peptide bond after the lysine residue. The enzyme can be used to cleave any fusion protein that carries this sequence. Recombinant Bovine Enterokinase is a single glycosylated polypeptide chain containing 235 amino acids and having an MW of ~28kDa.
Source
E. Coli.
Formulation
Bovine EK in 50mM Tris-HCl, pH 8.0, 0.5M NaCl and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Enteropeptidase or enterokinase is an enzyme involved in human digestion. It is produced by cells in the duodenum wall, and is secreted from duodenum's glands, the crypts of Lieberk?hn, whenever ingested food enters the duodenum from the stomach. Enteropeptidase has the critical job of turning trypsinogen (a zymogen) to trypsin, indirectly activating a number of pancreatic digestive enzymes. Enteropeptidase is a serine protease enzyme (EC 3.4.21.9). Enteropeptidase is a part of the Chymotrypsin-clan of serine proteases, and is structurally similar to these proteins.
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Synonyms
Enteropeptidase, EC 3.4.21.9, Enterokinase, Serine protease 7, ENTK, MGC133046.
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Physical Appearance
Sterile liquid solution.
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Stability
One year when stored at –20°C. Please avoid freeze-thaw cycles.
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Unit Definition
One unit is defined as the amount of enzyme needed to cleave 50µg of fusion protein in 16 hours to 95% completion at 25°C in a buffer containing 25mM Tris-HCl, pH 7.6, 50mM NaCl, and 2mM CaCl2.
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 :
OmpADescription:
Outer Membrane Protein-A Bacterial Recombinant
Outer Membrane Protein-A, OmpA.
Product # :
PRO-571Price :
Quantity :
Shipping Method :
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Description
The recombinant form was found to be undistinguishable from the wild type when examined by SDS-PAGE and gel filtration chromatography yielding a 50.5 kDa monomeric protein. The immunological similarity of the protein samples was demonstrated by employing polyclonal and monoclonal antibodies in ELISA and Western Blot techniques. All forms of A-protein were found to activate the secretion of tumour necrosis factor alpha from murine macrophage. For ref see Maurice et al. (1999) Protein Expression and Purification 16, 396-404.The OmpA is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The OmpA protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by Gel filtration.
(b) Analysis by SDS-PAGE.Biological Activity
The interaction of bacterial and recombinant A-layer protein with murine macrophages was directed at determining the effect of A-protein on intracellular events that occur in primed macrophages. This was accomplished by measuring the cytotoxic product produced by peritoneal macrophages when exposed to A-protein coated latex beads. Thioglycolate elicited macrophages exhibited a low level of activation (18% cytotoxicity) that was significantly increased (48% cytotoxicity) in the presence of latex beads. Coating of the latex beads with each of the three A-protein products resulted in an increase of cytoxicity (mean +/- SEM) from 48% to 91%.More Info
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Introduction
The OmpA protein is one of the main outer-membrane proteins of a large array of Gram-negative bacteria such as A.salmonicida, Shigella dysenteriae and E.coli.OmpA’s major physiological functions include maintenance of the structural integrity and morphology of the cells and porin activity, as well as a role in conjugation and bacteriophage binding.Achromogenic atypical Aeromonas salmonicida is the causative agent of goldfish ulcer disease.Virulence of this bacterium is associated with the production of a paracrystalline outer membrane A-layer protein.The species specific structural gene for the monomeric form of A-protein was cloned into a pET-3d plasmid in order to express and produce a recombinant form of the protein in E.coli BL21(DE3). The induced protein was isolated from inclusion bodies by a simple solubilization-renaturation procedure and purified by ion exchange chromatography on Q-Sepharose to over 95% pure monomeric protein.Recombinant A-protein was compared by biochemical, immunological and molecular methods with the A-protein isolated from atypical A.salmonicida bacterial cells by the glycine and the membrane extraction methods.
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Synonyms
Outer Membrane Protein-A, OmpA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Bacterial Outer Membrane Protein-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon C between 2-7 days and for future use reconstituted OmpA should be stored at 4 below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please avoid freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized OmpA in sterile 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
mdvvispndn tfvttslasv tkqpvldfst aqqnltlnfs evgdlknngf ivleiqgegq fndaeirqwl sngfwrrpft gllvnpndhg nfansgevnd vrkffkiisd gtqltivhti dsngkrlrla lasdveetin fadaevelkl nlanqafklt sgsqgtvalt agalwnasyt adpvatkplf klgklfqlsl tnagkatalv segflklnig danisatdfa itnvttnqti qrdkvnltlt gdvsafkkda ngnlvnkaga sigwkaaadg qsatavlgag nmaggvqnal aafgtlyvaa dntvpvpavn fnvkaeiqgd sqatynyfkd eladlfiltr dgmkfdtitt gttsanlihi rdvsnilpte ggkifvtite yadhaangrg egtvlvtrka lsvtlpsgga vtlkpadvaa dvgasitagr qarlvfevet nqgevavkks naegvdiqng trgtaplvdf tl.
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 :
Leptin Ovine, MTSDescription:
Leptin Ovine Recombinant, MTS tag
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-531Price :
Quantity :
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Shipped at Room temp
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Description
Leptin Ovine MTS tagged Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17.5 kDa.The Leptin is purified by proprietary chromatographic techniques. The membrane translocating sequence Tag is composed of 10 amino acids Val-Leu-Leu-Pro-Val-Leu-Leu-Ala-Ala-Pro located at the N-terminus.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.More Info
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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin Ovine MTS tagged although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Leptin in sterile 0.02% NaHCO3 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-Val-Leu-Leu-Pro.
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Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.18 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.
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Name :
CRP CanineDescription:
C-Reactive Protein Canine Recombinant
C-reactive protein, CRP, PTX1, MGC88244, MGC149895.
Product # :
PRO-2663Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CRP Canine Recombinant is a single, glycosylated polypeptide chain containing 204 amino acids and having a molecular mass of 23.2kDa (calculated).
Source
HEK293 cells.
Formulation
CRP filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20mM Tris, 50mM NaCl and 1mM CaCl2, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CRP is an acute phase protein that correlates with inflammatory disease and is synthesized by hepatocytes during the acute phase response by certain cytokines (IL-1 and TNF Alpha and Beta). CRP levels increase dramatically and serve as a useful marker of inflammation in such conditions as bacterial infection, rheumatoid arthritis, viral infections, transplantation rejection, meningitis, myocardial infarction, septicemia, osteomyelitis and others. CRP is also highly correlated to Serum Amyloid A levels.
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Synonyms
C-reactive protein, CRP, PTX1, MGC88244, MGC149895.
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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
QIDLDEKAFV FPRESENSYV ILFPQLQKPM KAFTVCLQVY TDLTRPHSLF SYATKSQSNE ILLFKERPGL FSVSVGGSDA FINFPQKFYA PQHFCVTWES VTGLTELWVD GKPMVRASLR RGYTVGSGAS IVLGQEQDSF GGGFDKNQSL VGDIEDVNMW DFVLSPSQIL TLYTTRALSP NVLNWRNLRY ETRGEVFLKK ELWS
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 :
NOV Human, HEKDescription:
Nephroblastoma Overexpressed Human Recombinant, HEK
Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.
Product # :
CYT-1032Price :
Quantity :
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Shipped at Room temp
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Description
NOV Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 33-357) containing 331 amino acids including a 6 a.a C-terminal His tag. The total molecular mass is 36.5kDa (calculated).
Source
HEK293 cells.
Formulation
NOV filtered (0.4 µm) and lyophilized from 0.5mg/ml in PBS and 5 % (w/v) trehalose.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Nephroblastoma Overexpressed (NOV) which is encoded by the NOV gene is a part of the CCN (CTGF/CYR61/NOV) family. NOV takes part in reducing tumorgenicity and proliferation of certain cancer cell lines. NOV interacts with numerous proteins and is involved in both internal and external cell signaling. NOV is expressed in particular tumors, including Wilm’s tumor and most nephroblastomas and is also exerts proangiogenic activities.
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Synonyms
Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.
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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 one week 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. NOV is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
QRCPPQCPGR CPATPPTCAP GVRAVLDGCS CCLVCARQRG ESCSDLEPCD ESSGLYCDRS ADPSNQTGIC TAVEGDNCVF DGVIYRSGEK FQPSCKFQCT CRDGQIGCVP RCQLDVLLPE PNCPAPRKVE VPGECCEKWI CGPDEEDSLG GLTLAAYRPE ATLGVEVSDS SVNCIEQTTE WTACSKSCGM GFSTRVTNRN RQCEMLKQTR LCMVRPCEQE PEQPTDKKGK KCLRTKKSLK AIHLQFKNCT SLHTYKPRFC GVCSDGRCCT PHNTKTIQAE FQCSPGQIVK KPVMVIGTCT CHTNCPKNNE AFLQELELKT TRGKMHHHHH H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CDH2 HumanDescription:
Cadherin 2 Human Recombinant
Cadherin 2, Cadherin 2, Type 1, N-Cadherin (Neuronal), Neural Cadherin, N-Cadherin, CDw325, NCAD, CDHN, Calcium-Dependent Adhesion Protein, Neuronal, CD325 Antigen, N-Cadherin 1, Cadherin-2, CD325.
Product # :
PRO-2455Price :
Quantity :
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Shipped with Ice Packs
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Description
CDH2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 574 amino acids (160-724a.a.) and having a molecular mass of 62.9kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).CDH2 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CDH2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Cadherin-2 isoform 1, also known as CDH2 is a transmembrane, homophilic glycoprotein which belongs to the calcium-dependent cell adhesion molecule family. CDH2 takes part in neurons and later on was discovered to participate in cardiac muscle and in cancer metastasis as well. The CDH2 loss promotes tumorigenesis through releasing membrane-bound β-catenin, and so stimulating Wnt signaling. Furthermore, CDH2 appears to be implicated in tumor development, however this discovery is limited in adrenocortical tumors-ACTs.
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Synonyms
Cadherin 2, Cadherin 2, Type 1, N-Cadherin (Neuronal), Neural Cadherin, N-Cadherin, CDw325, NCAD, CDHN, Calcium-Dependent Adhesion Protein, Neuronal, CD325 Antigen, N-Cadherin 1, Cadherin-2, CD325.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPDWVIPPI NLPENSRGPF PQELVRIRSD RDKNLSLRYS VTGPGADQPP TGIFIINPIS GQLSVTKPLD REQIARFHLR AHAVDINGNQ VENPIDIVIN VIDMNDNRPE FLHQVWNGTV PEGSKPGTYV MTVTAIDADD PNALNGMLRY RIVSQAPSTP SPNMFTINNE TGDIITVAAG LDREKVQQYT LIIQATDMEG NPTYGLSNTA TAVITVTDVN DNPPEFTAMT FYGEVPENRV DIIVANLTVT DKDQPHTPAW NAVYRISGGD PTGRFAIQTD PNSNDGLVTV VKPIDFETNR MFVLTVAAEN QVPLAKGIQH PPQSTATVSV TVIDVNENPY FAPNPKIIRQ EEGLHAGTML TTFTAQDPDR YMQQNIRYTK LSDPANWLKI DPVNGQITTI AVLDRESPNV KNNIYNATFL ASDNGIPPMS GTGTLQIYLL DINDNAPQVL PQEAETCETP DPNSINITAL DYDIDPNAGP FAFDLPLSPV TIKRNWTITR LNGDFAQLNL KIKFLEAGIY EVPIIITDSG NPPKSNISIL RVKVCQCDSN GDCTDVDRIV GAGLGTGAHH HHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CEACAM8 HumanDescription:
Carcinoembryonic Antigen-Related Cell Adhesion Molecule 8 Human Recombinant
Carcinoembryonic antigen-related cell adhesion molecule 8, CD67 antigen, Carcinoembryonic antigen CGM6, Non-specific cross-reacting antigen NCA-95, CD66b, CGM6, CD67, NCA-95, CEACAM8
Product # :
PRO-2716Price :
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Shipped with Ice Packs
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Description
CEACAM8 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 292 amino acids (35-320 a.a) and having a molecular mass of 32.3kDa.CEACAM8 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The CEACAM8 solution (1mg/1ml) 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
Carcinoembryonic Antigen-Related Cell Adhesion Molecule 8 (CEACAM8) is a cell surface glycoprotein which takes part in cell adhesion in a calciumindependent manner.CEACAM8mediates heterophilic cell adhesion with other carcinoembryonic antigen-related celladhesion molecules (CEACAM6 for example).CEACAM8main role is cell migration,cell adhesion, and pathogen binding.CEACAM-8 isexpressed mainly on the surface of human peripheral blood eosinophils isolated from healthy individuals andused as granulocyte marker.
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Synonyms
Carcinoembryonic antigen-related cell adhesion molecule 8, CD67 antigen, Carcinoembryonic antigen CGM6, Non-specific cross-reacting antigen NCA-95, CD66b, CGM6, CD67, NCA-95, CEACAM8
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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
QLTIEAVPSN AAEGKEVLLL VHNLPQDPRG YNWYKGETVD ANRRIIGYVI SNQQITPGPA YSNRETIYPN ASLLMRNVTR NDTGSYTLQV IKLNLMSEEV TGQFSVHPET PKPSISSNNS NPVEDKDAVA FTCEPETQNT TYLWWVNGQS LPVSPRLQLS NGNRTLTLLS VTRNDVGPYE CEIQNPASAN FSDPVTLNVL YGPDAPTISP SDTYYHAGVN LNLSCHAASN PPSQYSWSVN GTFQQYTQKL FIPNITTKNS GSYACHTTNS ATGRNRTTVR MITVSDHHHH HH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CXCL7 95 a.a HumanDescription:
Neutrophil Activating Protein-2 (CXCL7) Human Recombinant, 95 a.a.
Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.
Product # :
CHM-277Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NAP 2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 95 amino acids (35-128) and having a molecular mass of 10.3 kDa.The NAP 2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NAP 2 protein 1mg/ml is supplied in 20mM Tris-HCL, pH-7.5, 1mM DTT and 10% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Chemokine (C-X-C motif) ligand (CXCL7) is a small cytokine belonging to the CXC chemokine family. It is a protein that is released in large amounts from platelets following their activation. It stimulates various processes including mitogenesis, synthesis of extracellular matrix, glucose metabolism and synthesis of plasminogen activator.
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Synonyms
Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.
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Physical Appearance
NAP 2 is supplied as a sterile filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MSSTKGQTKR NLAKGKEESL DSDLYAELRC MCIKTTSGIH PKNIQSLEVI GKGTHCNQVE VIATLKDGRK ICLDPDAPRI KKIVQKKLAG DESAD
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Background
What is the molecular weight/Mw of CXCL7 95 A.A HUMAN Protein?
CXCL7 95 A.A HUMAN Protein has a total Mw of 10.3kDa.
What is the source or expression system of CXCL7 95 A.A HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL7 95 A.A HUMAN Protein?
CXCL7 95 A.A HUMAN Protein is > 90% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL7 95 A.A HUMAN Protein?
The biological functionality of CXCL7 95 A.A HUMAN Protein will be determined in the future.
What is the amino acid sequence of CXCL7 95 A.A HUMAN Protein?
MSSTKGQTKR NLAKGKEESL DSDLYAELRC MCIKTTSGIH PKNIQSLEVI GKGTHCNQVE VIATLKDGRK ICLDPDAPRI KKIVQKKLAG DESAD
What applications can CXCL7 95 A.A HUMAN Protein be used in?
CXCL7 95 A.A HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL7 95 A.A HUMAN Protein?
The endotoxin level is minimal, CXCL7 95 A.A 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 :
CA8 HumanDescription:
Carbonic Anhydrase 8 Human Recombinant
Carbonic anhydrase VIII, CALS, CARP, CA-VIII, CAMRQ3, CA-related protein, carbonate dehydratase, carbonic anhydrase-like sequence, carbonic anhydrase-related protein.
Product # :
ENZ-235Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CA8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 314 amino acids (1-290) and having a molecular mass of 35.5kDa.CA8 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CA8 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
CA8 was first called CA-related protein since there is a sequence similarity to other identified carbonic anhydrase genes. Still, this protein has no carbonic anhydrase activity - the reversible hydration of carbon dioxide. CA8 still holds a carbonic anhydrase designation due to obvious sequence similarity to other members of the carbonic anhydrase gene family. Mutations in CA8 result in cerebellar ataxia mental retardation and dysequilibrium syndrome type 3 (CMARQ3).
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Synonyms
Carbonic anhydrase VIII, CALS, CARP, CA-VIII, CAMRQ3, CA-related protein, carbonate dehydratase, carbonic anhydrase-like sequence, carbonic anhydrase-related protein.
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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 MGSHMADLSF IEDTVAFPEK EEDEEEEEEG VEWGYEEGVE WGLVFPDANG EYQSPINLNS REARYDPSLL DVRLSPNYVV CRDCEVTNDG HTIQVILKSK SVLSGGPLPQ GHEFELYEVR FHWGRENQRG SEHTVNFKAF PMELHLIHWN STLFGSIDEA VGKPHGIAII ALFVQIGKEH VGLKAVTEIL QDIQYKGKSK TIPCFNPNTL LPDPLLRDYW VYEGSLTIPP CSEGVTWILF RYPLTISQLQ IEEFRRLRTH VKGAELVEGC DGILGDNFRP TQPLSDRVIR AAFQ
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 :
CDNF MouseDescription:
Cerebral Dopamine Neurotrophic Factor Mouse Recombinant
Cerebral dopamine neurotrophic factor, ARMET-like protein 1, Conserved dopamine neurotrophic factor, Cdnf, Armetl1, 9330140G23.
Product # :
CYT-729Price :
Quantity :
Shipping Method :
Shipped at Room temp
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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.More Info
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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.
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Synonyms
Cerebral dopamine neurotrophic factor, ARMET-like protein 1, Conserved dopamine neurotrophic factor, Cdnf, Armetl1, 9330140G23.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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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.
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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.
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Amino Acid Sequence
QGLEAGVGPR ADCEVCKEFL DRFYNSLLSR GIDFSADTIE KELLNFCSDA KGKENRLCYY LGATTDAATK ILGEVTRPMS VHIPAVKICE KLKKMDSQIC ELKYGKKLDL ASVDLWKMRV AELKQILQRW GEECRACAEK SDYVNLIREL APKYVEIYPQ TEL.
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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.
- View Data Sheet
Description:
Leptin Super Antagonist Human Recombinant
Product # :
CYT-1238Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Super Leptin Antagonist Human Recombinant is a single polypeptide chain containing 146 amino acids. Super Human Leptin Antagonist was mutated, resulting in D23L/L39A/D40A/F41A super human leptin antagonist that was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (1mg/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
ProSpec’s super human leptin antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin.
More Info
-
Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Super Leptin Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution of super human leptin antagonist at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization super human leptin antagonist 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 Super Leptin Antagonist 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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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.
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Background
Leptin is a hormone which takes part in regulating body weight, metabolism and reproductive function. Leptin is a~16 kDa protein which is encoded by the obese gene. leptin is expressed predominantly by adipocytes, which fits with the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are highly expressed in areas of the hypothalamus which regulates body weight, as well as in T lymphocytes and vascular endothelial cells.
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 :
GSTK1 HumanDescription:
Glutathione S-Transferase Kappa 1 Human Recombinant
GST13, GST13-13, GSTK1-1, GST class-kappa, EC 2.5.1.18, Glutathione S-transferase kappa 1, Glutathione S-transferase subunit 13, hGSTK1, GSTK1.
Product # :
ENZ-476Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GSTK1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 226 amino acids (1-226 a.a.) and having a molecular mass of 25.5 kDa. GSTK1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GSTK1 solution containing 20mM Tris pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
GSTK1 is involved in cellular detoxification. GSTK1 is localized to the peroxisome and catalyzes the conjugation of the thiol group of glutathione (GSH) to the electrophilic groups of a broad range of hydrophobic substrates, leading to an easier removal of the latter from the cells.
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Synonyms
GST13, GST13-13, GSTK1-1, GST class-kappa, EC 2.5.1.18, Glutathione S-transferase kappa 1, Glutathione S-transferase subunit 13, hGSTK1, GSTK1.
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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
MGPLPRTVEL FYDVLSPYSW LGFEILCRYQ NIWNINLQLR PSLITGIMKD SGNKPPGLLP RKGLYMANDL KLLRHHLQIP IHFPKDFLSV MLEKGSLSAM RFLTAVNLEH PEMLEKASRE LWMRVWSRNE DITEPQSILA AAEKAGMSAE QAQGLLEKIA TPKVKNQLKE TTEAACRYGA FGLPITVAHV DGQTHMLFGS DRMELLAHLL GEKWMGPIPP AVNARL.
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 :
PDPN P56F7AT AntibodyDescription:
Podoplanin clone P56F7AT, Mouse Anti Human
Podoplanin, Glycoprotein 36, PA2.26 antigen, T1A, GP36, GP40, Gp38, OTS8, T1A2, HT1A-1, PA2.26, T1-alpha, PDPN.
Product # :
ANT-641Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
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Introduction
Podoplanin is a small mucin-like type-1 transmembrane protein, typically expressed in various specialized cell types throughout the body. Podoplanin is a type-I integral membrane glycoprotein with diverse distribution in human tissues. PDPN physiological function is related to its mucin-type character. The homologous protein in other species has been described as a differentiation antigen and influenza-virus receptor.
PDPN is expressed in lymphatic progenitor cells and afterwards during mouse development in lymphatic endothelial cells. Podoplanin is a specific marker for lymph vessel endothelial cells. Over-expression of podoplanin significantly elevates endothelial cell adhesion, migration, and tube formation. Inhibition of Podoplanin expression decreases cell adhesion in human dermal lymphatic endothelial cells. Podoplanin is used as a specific marker for lymphatic endothelium in histopathology.
Podoplanin expression is increased in nearly all human colon, rectum, and small intestine tumors. AGGRUS may serve as a diagnostic marker that distinguishes seminomas, the majority of which over express the protein, from embryonal carcinoma in testicular germ cell tumors. -
Synonyms
Podoplanin, Glycoprotein 36, PA2.26 antigen, T1A, GP36, GP40, Gp38, OTS8, T1A2, HT1A-1, PA2.26, T1-alpha, PDPN.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human PDPN mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human PDPN amino acids 99-207 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and k light chain.
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Clone
P56F7AT.
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Applications
PDPN antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
PDPN antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
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 :
MMP2 HumanDescription:
Matrix Metalloproteinase-2 Human Recombinant
kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, MMP-2, TBE-1, MMP2, CLG4A, CLG4, MONA, MMP-II.
Product # :
ENZ-769Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MMP2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 576 amino acids (110-660a.a) and having a molecular mass of 64.7kDa. MMP2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MMP2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Matrix metalloproteinase-2 (MMP-2) is involved in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response. MMP-2 contains a number of distinct domains: a prodomain that is cleaved upon activation; a catalytic domain containing the zinc binding site; a fibronectin like domain believed to have a role in substrate targeting; and a carboxyl terminal (hemopexin like) domain containing 2 N-linked glycosylation. The MMP-2 can degrade an extensive array of substrates including type IV, V, VII and X collagens as well as gelatin type I. In addition, MMP-2 interacts with THBS2, TIMP2, Thrombospondin 1, CCL7 and TIMP4. MMP-2 autocatalytic cleavage in the C-terminal generates the anti-angiogenic peptide, PEX. This process seems to be made possible by binding integrinv/beta3. Defects in the MMP-2 are the cause of Torg-Winchester syndrome (TWS), aka multicentric osteolysis nodulosis and arthropathy (MONA).
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Synonyms
kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, MMP-2, TBE-1, MMP2, CLG4A, CLG4, MONA, MMP-II.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSEFYNFFP RKPKWDKNQI TYRIIGYTPD LDPETVDDAF ARAFQVWSDV TPLRFSRIHD GEADIMINFG RWEHGDGYPF DGKDGLLAHA FAPGTGVGGD SHFDDDELWT LGEGQVVRVK YGNADGEYCK FPFLFNGKEY NSCTDTGRSD GFLWCSTTYN FEKDGKYGFC PHEALFTMGG NAEGQPCKFP FRFQGTSYDS CTTEGRTDGY RWCGTTEDYD RDKKYGFCPE TAMSTVGGNS EGAPCVFPFT FLGNKYESCT SAGRSDGKMW CATTANYDDD RKWGFCPDQG YSLFLVAAHE FGHAMGLEHS QDPGALMAPI YTYTKNFRLS QDDIKGIQEL YGASPDIDLG TGPTPTLGPV TPEICKQDIV FDGIAQIRGE IFFFKDRFIW RTVTPRDKPM GPLLVATFWP ELPEKIDAVY EAPQEEKAVF FAGNEYWIYS ASTLERGYPK PLTSLGLPPD VQRVDAAFNW SKNKKTYIFA GDKFWRYNEV KKKMDPGFPK LIADAWNAIP DNLDAVVDLQ GGGHSYFFKG AYYLKLENQS LKSVKFGSIK SDWLGC.
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 :
CRTAP HumanDescription:
Cartilage Associated Protein Human Recombinant
CASP, LEPREL3, OI7, Cartilage-associated protein, CRTAP.
Product # :
PRO-1862Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CRTAP Human Recombinant produced in E. coli is. a single polypeptide chain containing 398 amino acids (27-401) and having a molecular mass of 46.4kDa. CRTAP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CRTAP solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
Cartilage-associated protein (CRTAP) is a secreted protein localizing to the extracellular space which takes part in collagen post-translational modifications, extracellular fibril assembly and intracellular trafficking. CRTAP which is mainly expressed with predominant expression in articular chondrocytes is essential for efficient 3-hydroxylation of fibrillar collagen prolyl residues. Mutations in the gene encoding CRTAP might cause to autosomal recessive osteogenesis imperfecta (OI) type 7 and type 2B.
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Synonyms
CASP, LEPREL3, OI7, Cartilage-associated protein, CRTAP.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSQYERYSF RSFPRDELMP LESAYRHALD KYSGEHWAES VGYLEISLRL HRLLRDSEAF CHRNCSAAPQ PEPAAGLASY PELRLFGGLL RRAHCLKRCK QGLPAFRQSQ PSREVLADFQ RREPYKFLQF AYFKANNLPK AIAAAHTFLL KHPDDEMMKR NMAYYKSLPG AEDYIKDLET KSYESLFIRA VRAYNGENWR TSITDMELAL PDFFKAFYEC LAACEGSREI KDFKDFYLSI ADHYVEVLEC KIQCEENLTP VIGGYPVEKF VATMYHYLQF AYYKLNDLKN AAPCAVSYLL FDQNDKVMQQ NLVYYQYHRD TWGLSDEHFQ PRPEAVQFFN VTTLQKELYD FAKENIMDDD EGEVVEYVDD LLELEETS.
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 :
KLK7 Human, sf9Description:
Kallikrein-7 Human Recombinant, sf9
Kallikrein Related Peptidase 7, Kallikrein 7 (Chymotryptic, Stratum Corneum), Stratum Corneum Chymotryptic Enzyme, Serine Protease 6, PRSS6, SCCE, HK7, Kallikrein-Related Peptidase 7, Signal Protein, EC 3.4.21.117, EC 3.4.21, HSCCE.
Product # :
ENZ-962Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
KLK7 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 190 amino acids (1-181 a.a.) and having a molecular mass of 20.9kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions). KLK7 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
KLK7 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
KLK7 catalyzes the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. KLK7 cleaves insulin B chain at ''6-Leu- -Cys-7'', ''16-Tyr- -Leu-17'', ''25-Phe- -Tyr-26'' and ''26-Tyr--Thr-27''. KLK7 is involved in the activation of precursors to inflammatory cytokines.
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Synonyms
Kallikrein Related Peptidase 7, Kallikrein 7 (Chymotryptic, Stratum Corneum), Stratum Corneum Chymotryptic Enzyme, Serine Protease 6, PRSS6, SCCE, HK7, Kallikrein-Related Peptidase 7, Signal Protein, EC 3.4.21.117, EC 3.4.21, HSCCE.
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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
ADPMNEYTVH LGSDTLGDRR AQRIKASKSF RHPGYSTQTH VNDLMLVKLN SQARLSSMVK KVRLPSRCEP PGTTCTVSGW GTTTSPDVTF PSDLMCVDVK LISPQDCTKV YKDLLENSML CAGIPDSKKN ACNGDSGGPL VCRGTLQGLV SWGTFPCGQP NDPGVYTQVC KFTKWINDTM KKHRHHHHHH.
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 :
HERPUD1 HumanDescription:
HERPUD1 Human Recombinant
Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein, HERPUD1, Methyl methanesulfonate (MMF)-inducible fragment protein 1, HERP, KIAA0025, MIF1, Mif1, SUP.
Product # :
PRO-2105Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HERPUD1 Human Recombinant produced in E. coli is a single polypeptide chain containing 286 amino acids (1-263) and having a molecular mass of 31.6kDa.HERPUD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HERPUD1 solution (0.5mg/1ml) contains Phosphate buffer saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
HERPUD1 is a multi-pass membrane protein which is a part of the endoplasmic reticulum quality control system. HERPUD1 owns 1 N-terminal ubiquitin-like domain and is expressed highly in the brain. HERPUD1 is also known as ER-associated degradation (ERAD) which takes part in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins.
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Synonyms
Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein, HERPUD1, Methyl methanesulfonate (MMF)-inducible fragment protein 1, HERP, KIAA0025, MIF1, Mif1, SUP.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMESETEP EPVTLLVKSP NQRHRDLELS GDRGWSVGHL KAHLSRVYPE RPRPEDQRLI YSGKLLLDHQ CLRDLLPKQE KRHVLHLVCN VKSPSKMPEI NAKVAESTEE PAGSNRGQYP EDSSSDGLRQ REVLRNLSSP GWENISRPEA AQQAFQGLGP GFSGYTPYGW LQLSWFQQIY ARQYYMQYLA ATAASGAFVP PPSAQEIPVV SAPAPAPIHN QFPAENQPAN QNAAPQVVVN PGANQNLRMN AQGGPIVEED DEINRD.
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 :
SERPINF2 MouseDescription:
Serpin Peptidase Inhibitor, Clade F Member 2 Mouse Recombinant
Alpha-2-antiplasmin, Alpha-2-AP, Alpha-2-plasmin inhibitor, Alpha-2-PI, Serpin F2.
Product # :
PRO-2240Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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Description
SERPINF2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 470 amino acids (28-491 a.a.) and having a molecular mass of 52.9kDa (Migrates at 70-100kDa on SDS-PAGE under reducing conditions). SERPINF2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
SERPINF2 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Alpha-2-antiplasmin (SERPINF2) is a serine protease inhibitor. The main targets of SERPINF2 are plasmin and trypsin; however SERPINF2 also inactivates matriptase-3/TMPRSS7 and chymotrypsin.
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Synonyms
Alpha-2-antiplasmin, Alpha-2-AP, Alpha-2-plasmin inhibitor, Alpha-2-PI, Serpin F2.
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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
VDLPGQQPVS EQAQQKLPLP ALFKLDNQDF GDHATLKRSP GHCKSVPTAE ETRRLAQAMM AFTTDLFSLV AQTSTSSNLV LSPLSVALAL SHLALGAQNQ TLHSLHRVLH MNTGSCLPHL LSHFYQNLGP GTIRLAARIY LQKGFPIKDD FLEQSERLFG AKPVKLTGKQ EEDLANINQW VKEATEGKIE DFLSELPDST VLLLLNAIHF HGFWRTKFDP SLTQKDFFHL DERFTVSVDM MHAVSYPLRW FLLEQPEIQV AHFPFKNNMS FVVVMPTYFE WNVSEVLANL TWDTLYHPSL QERPTKVWLP KLHLQQQLDL VATLSQLGLQ ELFQGPDLRG ISEQNLVVSS VQHQSTMELS EAGVEAAAAT SVAMNRMSLS SFTVNRPFLF FIMEDTIGVP LFVGSVRNPN PSALPQLQEQ RDSPDNRLIG QNDKADFHGG KTFGPDLKLA PRMEEDYPQF SSPKHHHHHH.
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 :
LGALS2 Mouse, ActiveDescription:
Galectin-2, BioActive Mouse Recombinant
Galectin-2, Gal-2, Lgals2, 2200008F12Rik, AI324147.
Product # :
CYT-1155Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LGALS2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids (1-130 a.a) and having a molecular mass of 17.3kDa.LGALS2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
LGALS2 protein (1mg/ml) contains 10% glycerol, 0.1M NaCl, 1mM DTT and 20mM Tris-HCl buffer (pH 8.0).
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Measured by its ability to agglutinate human red blood cells. The ED50 is ≥ 20ug/ml.
More Info
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Introduction
Galectin-2 or LGALS2 is a protein, part of the galectin proteins family. The galectin proteins family holds galectin proteins family lectins that mediates adhesion between cells or cells to ECM. This family also take part in pre-mRNA splicing, apoptosis & tumor progression. Galectin-2 induces apoptosis in T cells that are activated & binds to lymphotoxin-a, also can implicatate on myocardial infarction. LGALS2 from human and mouse share about 65% amino acid sequence resemblance.
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Synonyms
Galectin-2, Gal-2, Lgals2, 2200008F12Rik, AI324147.
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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 MGSMSEKFEV KDLNMKPGMS LKIKGKIHND VDRFLINLGQ GKETLNLHFN PRFDESTIVC NTSEGGRWGQ EQRENHMCFS PGSEVKITIT FQDKDFKVTL PDGHQLTFPN RLGHNQLHYL SMGGLQISSF KLE
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Background
What is the molecular weight/Mw of LGALS2 MOUSE, ACTIVE Protein?
LGALS2 MOUSE, ACTIVE Protein has a total Mw of 17.3kDa.
What is the source or expression system of LGALS2 MOUSE, ACTIVE Protein?
Escherichia Coli.
What is the Purity of LGALS2 MOUSE, ACTIVE Protein?
LGALS2 MOUSE, ACTIVE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS2 MOUSE, ACTIVE Protein?
Measured by its ability to agglutinate human red blood cells. The ED50 is ≥ 20ug/ml.
What is the amino acid sequence of LGALS2 MOUSE, ACTIVE Protein?
MGSSHHHHHH SSGLVPRGSH MGSMSEKFEV KDLNMKPGMS LKIKGKIHND VDRFLINLGQ GKETLNLHFN PRFDESTIVC NTSEGGRWGQ EQRENHMCFS PGSEVKITIT FQDKDFKVTL PDGHQLTFPN RLGHNQLHYL SMGGLQISSF KLE.
What applications can LGALS2 MOUSE, ACTIVE Protein be used in?
LGALS2 MOUSE, ACTIVE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS2 MOUSE, ACTIVE Protein?
The endotoxin level is minimal, LGALS2 MOUSE, ACTIVE 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 :
LGALS7 HumanDescription:
Galectin-7 Human Recombinant
Galectin-7, Gal-7, HKL-14, PI7, p53-induced gene 1 protein, LGALS7, PIG1, LGALS7B, GAL7, LGALS7A.
Product # :
CYT-016Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Galectin-7 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 136 amino acids and having a molecular mass of 15kDa.The LGALS7 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LGALS7 was lyophilized from a concentrated (1mg/ml) solution in 20mM Tris, 150mM NaCl, 1mM EDTA and 5% Trehalose, pH 8.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Galectins are a family of animal lectins with an affinity for beta-galactosides. This family has at least 14 identified members. Galectins share similarities in the CRD (the carbohydrate recognition domain). Galectins are synthesized as cytosolic proteins. Though localized principally in the cytoplasm and lacking a classical signal peptide, galectins can also be stimulated to secretion by non-classical pathways or alternatively targeted to the nucleus. Galectins are involved in modulating cell-cell and cell-matrix interactions. Human Galectin-7 belongs to the prototypical Galectins containing a single CRD, which is initially identified in human epidermis as a monomer. The Galectin-7 expression is induced by tumor suppressor protein p53 and associated with apoptosis. Galectin-7 is a pro-apoptotic protein which functions intracellularlly upstream of JNK activation and mitochondrial cytochrome c release. The correlation of Galectin-7 with the UV-induced apoptosis of keratinocytes presents a critical mechanism in the maintenance of epidermal homeostasis. Human Galectin-7 is localized in both nucleus and cytoplasm.
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Synonyms
Galectin-7, Gal-7, HKL-14, PI7, p53-induced gene 1 protein, LGALS7, PIG1, LGALS7B, GAL7, LGALS7A.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized LGALS7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Galectin-7 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 Galectin-7 in sterile distilled H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MSNVPHKSSLPEGIRPGTVLRIRGLVPPNASRFHVNLLCGEEQGSDAALHFNP
RLDTSEVVFNSKEQGSWGREERGPGVPFQRGQPFEVLIIASDDGFKAVVGDAQ
YHHFRHRLPLARVRLVEVGGDVQLDSVRIF -
Background
What is the molecular weight/Mw of LGALS7 HUMAN Protein?
LGALS7 HUMAN Protein has a total Mw of 15kDa.
What is the source or expression system of LGALS7 HUMAN Protein?
Escherichia Coli.
What is the Purity of LGALS7 HUMAN Protein?
LGALS7 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS7 HUMAN Protein?
The biological functionality of LGALS7 HUMAN Protein will be determined in the future.
What is the amino acid sequence of LGALS7 HUMAN Protein?
MSNVPHKSSLPEGIRPGTVLRIRGLVPPNASRFHVNLLCGEEQGSDAALHFNP
RLDTSEVVFNSKEQGSWGREERGPGVPFQRGQPFEVLIIASDDGFKAVVGDAQ
YHHFRHRLPLARVRLVEVGGDVQLDSVRIF
What applications can LGALS7 HUMAN Protein be used in?
LGALS7 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS7 HUMAN Protein?
The endotoxin level is minimal, LGALS7 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 :
CNDP1 MouseDescription:
CNDP Dipeptidase 1 Mouse Recombinant
Beta-Ala-His dipeptidase, CNDP dipeptidase 1, Carnosine dipeptidase 1.
Product # :
ENZ-977Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
CNDP1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 500 amino acids (1-492 a.a.) and having a molecular mass of 56.1kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). CNDP1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CNDP1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CNDP Dipeptidase 1, also known as CNDP1 is a member of the peptidase M20A family. CNDP1 Mannheim which is the shortest allelic form has been more common in the absence of nephropathy in addition to being associated with lower serum carnosinase levels. Furthermore, Carnosine inhibited the increased production of fibronectin as well as collagen type VI in podocytes and the increased production of TGF-beta in mesangial cells. Diabetic patients with the CNDP1 Mannheim variant are less at risk for nephropathy. In addition, on renal cells carnosine protects against the adverse effects of high glucose levels.
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Synonyms
Beta-Ala-His dipeptidase, CNDP dipeptidase 1, Carnosine dipeptidase 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
MFSSAHSGLL EKLFHYIDLH QDEFVQTLKE WVAIESDSVQ PVPRLRQKLF QMMALAADKL RNLGAGVESI DLGSQQMPDG QSLPIPPILL AELGSDPEKP TVCFYGHLDV QPAQKDDGWL TDPYTLTEVD GKLYGRGATD NKGPVLAWIN AVSTFRALQQ DLPVNIKLIL EGMEEAGSIA LEELVMREKD HFFSSVDYIV ISDNLWLSQR KPALTYGTRG NCYFTVEVKC RDQDFHSGTF GGILNEPMAD LVALLGSLVD SSGHILIPGI YDQMAPITEG EKTMYKNIDM DLEEYQNINQ VEKFLFDTKE ELLMHLWRYP SLSIHGIEGA FDEPGTKTVI PGRVLGKFSI RLVPTMSPSV VEKQVTQHLE AVFSKRNSFN KMAVSMVLGL HPWTANVNDT QYLAAQRTIK TVFGVNPDMI RDGSTIPIAK IFQAITQKSV MMLPLGAVDD GEHSQNEKIN RWNYIQGSKL FAAFFLELSK QHSGHQMPSS VYLEHHHHHH.
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.