Search results
1000 results found for “epigen”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
sCD23 HumanDescription:
Soluble CD23 Human Recombinant
Low affinity immunoglobulin epsilon Fc receptor, Lymphocyte IgE receptor, Fc-epsilon-RII, BLAST-2, Immunoglobulin E-binding factor, CD23 antigen, FCER2, CD23, FCE2, CD23A, IGEBF, CLEC4J.
Product # :
PRO-1789Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
sCD23 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 172 amino acids and having a molecular mass of 19.2kDa.The sCD23 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 is determined by its ability to induce TNF-alpha production by human PBMCs.More Info
-
Introduction
CD23 is a 45kDa glycoprotein, which is present on a subpopulation of freshly isolated peripheral blood and tonsil B cells and strongly expressed on EBV-transformed B lymphoblasts. The CD23 molecule is identical to the low affinity IgE receptor found on B cells. Expression of CD23 has been detected in neoplastic cells from cases of B cell chronic lymphocyctic leukaemia and some cases of centroblastic/centrocytic lymphoma.
-
Synonyms
Low affinity immunoglobulin epsilon Fc receptor, Lymphocyte IgE receptor, Fc-epsilon-RII, BLAST-2, Immunoglobulin E-binding factor, CD23 antigen, FCER2, CD23, FCE2, CD23A, IGEBF, CLEC4J.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized sCD23 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution sCD23 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 sCD23 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MELQVSSGFV CNTCPEKWIN FQRKCYYFGK GTKQWVHARY ACDDMEGQLV SIHSPEEQDF LTKHASHTGS WIGLRNLDLK GEFIWVDGSH VDYSNWAPGE PTSRSQGEDC VMMRGSGRWN DAFCDRKLGA WVCDRLATCT PPASEGSAES MGPDSRPDPD GRLPTPSAPL HS
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 :
EBV p23Description:
Epstein-Barr Virus (HHV-4) p23 Recombinant
Product # :
EBV-274Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
The E.Coli derived recombinant protein contains the HHV-4 p23 regions, 1-162 amino acids and fused to a GST-Tag at C-terminus.
Source
Escherichia Coli.
Formulation
25mM glycine pH-9.6 and 50% glycerol.
Purity
EBV- p23 protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
-
Introduction
The Epstein-Barr virus (EBV), also called Human herpes virus 4 (HHV-4), is a virusof the herpes family(which includes Herpes simplex virusand Cytomegalovirus. On infecting the B-lymphocyte, the linear virus genome circularizes and the virus subsequently persists within the cell as an episome. The virus can execute several distinct programs of gene expressionwhich can be broadly categorized as being lytic cycle or latent cycle. The lytic cycleor productive infection results in staged expression of a host of viral proteinswith the ultimate objective of producing infectious virions. Formally, this phase of infection does not inevitably lead to lysis of the host cellas EBV virions are produced by budding from the infected cell. The latent cycle(lysogenic) programs are those that do not result in production of virions. A very limited, distinct set of viral proteins are produced during latent cycle infection. These include Epstein-Barr nuclear antigen(EBNA)-1, EBNA-2, EBNA-3A, EBNA-3B, EBNA-3C, EBNA-leader protein (EBNA-LP) and latent membrane proteins(LMP)-1, LMP-2A and LMP-2B and the Epstein-Barr encoded RNAs(EBERs).
-
Stability
EBV-p23 protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
-
Applications
EBV-p23 antigen is suitable for ELISA and Western blots, excellent antigen for detection of HHV-4 (EBV) with minimal specificity problems.
-
Specificity
Immunoreactive with sera of EBV-infected individuals.
-
Purification Method
EBV-p23 was purified by proprietary chromatographic technique.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
METRN MouseDescription:
Meteorin Mouse Recombinant
Meteorin, Hypoxia/reoxygenation regulatory factor, Metrn, 1810034B16Rik, Hyrac.
Product # :
PRO-2241Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
METRN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 276 amino acids (22-291 a.a.) and having a molecular mass of 30.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions). METRN is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
METRN protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Meteorin (METRN) is involved in both glial cell differentiation and axonal network formation during neurogenesis. METRN promotes astrocyte differentiation and transforms cerebellar astrocytes into radial glia. Moreover, the METRN protein stimulates axonal extension in small and intermediate neurons of sensory ganglia by activating nearby satellite glia.
-
Synonyms
Meteorin, Hypoxia/reoxygenation regulatory factor, Metrn, 1810034B16Rik, Hyrac.
-
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
GYSEDRCSWR GSGLTQEPGS VGQLTLDCTE GAIEWLYPAG ALRLTLGGPD PGTRPSIVCL RPERPFAGAQ VFAERMTGNL ELLLAEGPDL AGGRCMRWGP RERRALFLQA TPHRDISRRV AAFRFELHED QRAEMSPQAQ GLGVDGACRP CSDAELLLAA CTSDFVIHGT IHGVAHDTEL QESVITVVVA RVIRQTLPLF KEGSSEGQGR ASIRTLLRCG VRPGPGSFLF MGWSRFGEAW LGCAPRFQEF SRVYSAALTT HLNPCEMALD HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
EMCN HumanDescription:
Endomucin Human Recombinant
Endomucin, Endomucin-2, Gastric cancer antigen Ga34, Mucin-14, MUC-14, EMCN, EMCN2, MUC14.
Product # :
PRO-1156Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
EMCN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids (19-190 a.a) and having a molecular mass of 20.5kDa.EMCN is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
EMCN protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer, pH8.0, 10% glycerol, 1mM DTT and 100mM NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
Endothelial sialomucin (Endomucin) interferes with the assembly of focal adhesion complexes and inhibits interaction between cells and the extracellular matrix. Endomucin is expressed in the heart, kidney and lung.
-
Synonyms
Endomucin, Endomucin-2, Gastric cancer antigen Ga34, Mucin-14, MUC-14, EMCN, EMCN2, MUC14.
-
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 MGSHMNSTGV LEAANNSLVV TTTKPSITTP NTESLQKNVV TPTTGTTPKG TITNELLKMS LMSTATFLTS KDEGLKATTT DVRKNDSIIS NVTVTSVTLP NAVSTLQSSK PKTETQSSIK TTEIPGSVLQ PDASPSKTGT LTSIPVTIPE NTSQSQVIGT EGGKNASTSA TSRSYSS.
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 :
HB-EGF MouseDescription:
HB-EGF Mouse Recombinant
DTR, HEGFL, diphtheria toxin receptor, DTSF.
Product # :
CYT-068Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- sds-page
Description
HB-EGF Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids (63-148 a.a.) and having a molecular mass of 9.8 kDa.The HB-EGF is purified by proprietary chromatographic techniques
Source
Escherichia Coli.
Formulation
The protein was filtered (0.2µm) and lyophilized from a concentrated solution containing 10mM PB and 500mM NaCl, pH7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 was determined by a cell proliferation assay using balb/c 3T3 cells is < 1.0 ng/ml, corresponding to a specific activity of > 1.0×106 units/mg.sds-page
More Info
-
Introduction
HB-EGF is an EGF related growth factor which signals via the EGF receptor, and stimulates the proliferation of SMC (smooth muscle cells), fibroblasts, epithelial cells and keratinocytes. HB-EGF is expressed in various cell types and tissues, including vascular endothelial cells and SMC, macrophages, skeletal muscle, keratinocytes and particular tumor cells. HB-EGF’s ability to explicitly bind sulfate proteoglycans is dissimilar from other EGF-like molecules, and might be related to the enhanced mitogenic activity, relative to EGF, that HB-EGF exerts on smooth muscle cells.
-
Synonyms
DTR, HEGFL, diphtheria toxin receptor, DTSF.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Mouse HB-EGF Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HB-EGF 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 Mouse HB-EGF in sterile 18M-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
DLEGTDLNLF KVAFSSKPQG LATPSKERNG KKKKKGKGLG KKRDPCLRKY KDYCIHGECR YLQEFRTPSC KCLPGYHGHR CHGLTL.
-
Background
What is the molecular weight/Mw of HB-EGF Protein?
HB-EGF Protein has a total Mw of 9.8kDa.
What is the source or expression system of HB-EGF Protein?
Escherichia Coli.
What is the Purity of HB-EGF Protein?
HB-EGF Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of HB-EGF Protein?
The ED50 was determined by a cell proliferation assay using balb/c 3T3 cells is < 1.0 ng/ml, corresponding to a specific activity of > 1.0×106 units/mg.
What is the amino acid sequence of HB-EGF Protein?
DLEGTDLNLF KVAFSSKPQG LATPSKERNG KKKKKGKGLG KKRDPCLRKY KDYCIHGECR YLQEFRTPSC KCLPGYHGHR CHGLTL.
What applications can HB-EGF Protein be used in?
HB-EGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for HB-EGF Protein?
The endotoxin level is minimal, HB-EGF 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 :
Leptin tA OvineDescription:
Leptin Antagonist Triple Mutant Ovine Recombinant
Product # :
CYT-356Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Leptin Antagonist Triple Mutant Ovine Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A mutant. Leptin Antagonist Triple Mutant Ovine Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
ProSpec’s Leptin-Antagonist Triple Mutant Ovine Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of mouse leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.More Info
-
Physical Appearance
White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Leptin Antagonist Triple Mutant Ovine Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Lep-tA mutant mg/ml and up to 2 mM and filter sterilization Leptin mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Leptin-Antagonist Triple Mutant Ovine Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8, not less than 100µg/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 Ala-Val-Pro-Ile-Arg.
-
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.21 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
MIF HumanDescription:
Macrophage Migration Inhibitory Factor Human Recombinant
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
Product # :
CYT-575Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Macrophage Inducing Factor Human Recombinant produced in E. coli is a single, non-glycosylated, polypeptide chain containing 115 amino acids (1-115aa) and having a molecular mass of 12kDa. MIF human Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1mg/ml solution containing 50mM Tris-HCl pH-8, 0.5mM DTT & 10% glycerol.
Purity
Greater than 98.0% as determined by SDS-PAGE.
More Info
-
Introduction
The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.
-
Synonyms
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
-
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
MPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC SLHSIGKIGG AQNRSYSKLL CGLLAERLRI SPDRVYINYY DMNAANVGWN NSTFA.
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 :
SNTN HumanDescription:
Sentan Cilia Apical Structure Protein Human Recombinant
Sentan cilia apical structure protein, FLJ44379, S100AL, S100A1L, S100A-like protein, sentan, S100 calcium-binding protein A1-like.
Product # :
PRO-216Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
SNTN Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 167 amino acids (1-147a.a.) and having a molecular mass of 18.6kDa. The SNTN is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SNTN solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 50% glycerol and 0.15M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
SNTN is a member of to the S-100 family. SNTN is localized solely to the bridging structure between the cell membrane and peripheral singlet microtubules that specifically exists in the narrowed distal portion of cilia. Exogenously expressed sentan displayed affinity for the membrane protrusions, and a protein-lipid binding assay discovered that sentan bounds to phosphatidylserine which indicate that sentan is the leading molecular component of the ciliary tip to link the cell membrane and peripheral singlet microtubules, making the distal portion of the cilia narrow and stiff to permit better airway approval or ovum transport.
-
Synonyms
Sentan cilia apical structure protein, FLJ44379, S100AL, S100A1L, S100A-like protein, sentan, S100 calcium-binding protein A1-like.
-
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 MGGCMHSTQD KSLHLEGDPN PSAAPTSTCA PRKMPKRISI SKQLASVKAL RKCSDLEKAI ATTALIFRNS SDSDGKLEKA IAKDLLQTQF RNFAEGQETK PKYREILSEL DEHTENKLDF EDFMILLLSI TVMSDLLQNI RNVKIMK
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
EFNB2 HumanDescription:
Ephrin- B2 Human Recombinant
Ephrin-B2, EPH-related receptor tyrosine kinase ligand 5, LERK-5, HTK ligand, HTK-L, EFNB2, EPLG5, HTKL, LERK5, MGC126226, MGC126227, MGC126228.
Product # :
PRO-937Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
EFNB2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (28-229 a.a.) and having a molecular mass of 24.9kDa.EFNB2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
EFNB2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 20% glycerol and 200mM NaCl.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
Ephrin-B2 belongs to the ephrin (EPH) family. The ephrins and EPH-related receptors contain the largest subfamily of receptor protein-tyrosine kinases and have been associated with mediating developmental events, particularly in the nervous system and in erythropoiesis. Based upon their structures and sequence relationships, ephrins are allocated into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. Ephrin-B2 binds to the EPHB4 and EPHA3 receptors.
-
Synonyms
Ephrin-B2, EPH-related receptor tyrosine kinase ligand 5, LERK-5, HTK ligand, HTK-L, EFNB2, EPLG5, HTKL, LERK5, MGC126226, MGC126227, MGC126228.
-
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 MGSHMIVLEP IYWNSSNSKF LPGQGLVLYP QIGDKLDIIC PKVDSKTVGQ YEYYKVYMVD KDQADRCTIK KENTPLLNCA KPDQDIKFTI KFQEFSPNLW GLEFQKNKDY YIISTSNGSL EGLDNQEGGV CQTRAMKILM KVGQDASSAG STRNKDPTRR PELEAGTNGR SSTTSPFVKP NPGSSTDGNS AGHSGNNILG SEVALFA.
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 :
ELAVL2 HumanDescription:
ELAV Like Neuron-Specific RNA Binding Protein 2 Human Recombinant
ELAV Like Neuron-Specific RNA Binding Protein 2, HUB, ELAV (Embryonic Lethal, Abnormal Vision, Drosophila)-Like 2 (Hu Antigen B), Nervous System-Specific RNA-Binding Protein Hel-N1, Hu-Antigen B, HELN1, ELAV (Embryonic Lethal, Abnormal Vision, Drosophila)-Like 2, ELAV-Like Neuronal Protein 1 Isoform Hel-N2, ELAV-Like Neuronal Protein 1, ELAV-Like Protein 2, Hu Antigen B, HEL-N1, ELAV-like protein 2, ELAV-like neuronal protein 1, Hu-antigen B.
Product # :
PRO-2155Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
ELAVL2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 369 amino acids (1-346 a.a) and having a molecular mass of 40.4kDa. ELAVL2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ELAVL2 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
ELAV Like Neuron-Specific RNA Binding Protein 2, also known as ELAVL2 is a neural-specific RNA-binding protein which is recognized with his ability to bind to several 3' UTRs, as well as its own and in addition those of FOS and ID. ELAVL2 identify a GAAA motif in the RNA. One of the diseases associated with ELAVL2 is contagious pustular dermatitis.
-
Synonyms
ELAV Like Neuron-Specific RNA Binding Protein 2, HUB, ELAV (Embryonic Lethal, Abnormal Vision, Drosophila)-Like 2 (Hu Antigen B), Nervous System-Specific RNA-Binding Protein Hel-N1, Hu-Antigen B, HELN1, ELAV (Embryonic Lethal, Abnormal Vision, Drosophila)-Like 2, ELAV-Like Neuronal Protein 1 Isoform Hel-N2, ELAV-Like Neuronal Protein 1, ELAV-Like Protein 2, Hu Antigen B, HEL-N1, ELAV-like protein 2, ELAV-like neuronal protein 1, Hu-antigen B.
-
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 MGSMETQLSN GPTCNNTANG PTTINNNCSS PVDSGNTEDS KTNLIVNYLP QNMTQEELKS LFGSIGEIES CKLVRDKITG QSLGYGFVNY IDPKDAEKAI NTLNGLRLQT KTIKVSYARP SSASIRDANL YVSGLPKTMT QKELEQLFSQ YGRIITSRIL VDQVTGISRG VGFIRFDKRI EAEEAIKGLN GQKPPGATEP ITVKFANNPS QKTNQAILSQ LYQSPNRRYP GPLAQQAQRF RFSPMTIDGM TSLAGINIPG HPGTGWCIFV YNLAPDADES ILWQMFGPFG AVTNVKVIRD FNTNKCKGFG FVTMTNYDEA AMAIASLNGY RLGDRVLQVS FKTNKTHKA.
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 :
ELP4 HumanDescription:
Elongator Acetyltransferase Complex Subunit 4 Human Recombinant
Elongator complex protein 4, ELP4, Elongator Acetyltransferase Complex Subunit 4, hELP4, PAX6 neighbor gene protein, C11orf19, PAXNEB, dJ68P15A.1, PAX6NEB.
Product # :
PRO-2102Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
ELP4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 447 amino acids (1-424 a.a.) and having a molecular mass of 49kDa.ELP4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ELP4 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
-
Introduction
Elongator Acetyltransferase Complex Subunit 4, also known as ELP4 is a protein coding gene which is a subunit of the RNA polymerase II elongator complex. ELP4 complements phenotypes of yeast ELP4 deletion mutants and is related to Rolandic epilepsy.
-
Synonyms
Elongator complex protein 4, ELP4, Elongator Acetyltransferase Complex Subunit 4, hELP4, PAX6 neighbor gene protein, C11orf19, PAXNEB, dJ68P15A.1, PAX6NEB.
-
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 MGSMAAVATC GSVAASTGSA VATASKSNVT SFQRRGPRAS VTNDSGPRLV SIAGTRPSVR NGQLLVSTGL PALDQLLGGG LAVGTVLLIE EDKYNIYSPL LFKYFLAEGI VNGHTLLVAS AKEDPANILQ ELPAPLLDDK CKKEFDEDVY NHKTPESNIK MKIAWRYQLL PKMEIGPVSS SRFGHYYDAS KRMPQELIEA SNWHGFFLPE KISSTLKVEP CSLTPGYTKL LQFIQNIIYE EGFDGSNPQK KQRNILRIGI QNLGSPLWGD DICCAENGGN SHSLTKFLYV LRGLLRTSLS ACIITMPTHL IQNKAIIARV TTLSDVVVGL ESFIGSERET NPLYKDYHGL IHIRQIPRLN NLICDESDVK DLAFKLKRKL FTIERLHLPP DLSDTVSRSS KMDLAESAKR LGPGCGMMAG GKKHLDF.
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 :
PGK1 HumanDescription:
Phosphoglycerate Kinase 1 Human Recombinant
Phosphoglycerate kinase 1, Primer recognition protein 2, Cell migration-inducing gene 10 protein, PRP 2, PGKA, MIG10, MGC8947, MGC117307, MGC142128, PGK1.
Product # :
PKA-351Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
PGK1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 437 amino acids (1-417 a.a.) and having a molecular mass of 46.8kDa. PGK1 is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PGK1 solution containing 20mM Tris (pH 8.0), 10% Glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
PGK1 is an X-linked enzyme that has a major role in the glycolytic pathway. PGK1 is a glycolytic enzyme which catalyzes the conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate, generating an ATP molecule. PGK1 may also act as a cofactor for polymerase alpha. Defects in the PGK1 gene are usually associated with chronic hemolytic anemia, though it can be accompanied by either mental retardation or muscular disease (rhabdomyolysis). Overexpression of PGK1 and its signalling targets are possibly an expression-pathway in diffuse primary gastric carcinomas promoting peritoneal dissemination. It was shown that PGK1 is differentially expressed in the dorsolateral prefrontal cortex from patients with schizophrenia.
-
Synonyms
Phosphoglycerate kinase 1, Primer recognition protein 2, Cell migration-inducing gene 10 protein, PRP 2, PGKA, MIG10, MGC8947, MGC117307, MGC142128, PGK1.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
PGK1 although stable at 4°C for 1 week, should be stored 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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSLSNKLTLD KLDVKGKRVV MRVDFNVPMK NNQITNNQRI KAAVPSIKFC LDNGAKSVVL MSHLGRPDGV PMPDKYSLEP VAVELKSLLG KDVLFLKDCV GPEVEKACAN PAAGSVILLE NLRFHVEEEG KGKDASGNKV KAEPAKIEAF RASLSKLGDV YVNDAFGTAH RAHSSMVGVN LPQKAGGFLM KKELNYFAKA LESPERPFLA ILGGAKVADK IQLINNMLDK VNEMIIGGGM AFTFLKVLNN MEIGTSLFDE EGAKIVKDLM SKAEKNGVKI TLPVDFVTAD KFDENAKTGQ ATVASGIPAG WMGLDCGPES SKKYAEAVTR AKQIVWNGPV GVFEWEAFAR GTKALMDEVV KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKVLPG VDALSNI.
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 :
FIMC E.ColiDescription:
Chaperone Protein fimC E.Coli Recombinant
Chaperone protein fimC, fimC, b4316, JW4279.
Product # :
PRO-120Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
FIMC E.Coli Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 226 amino acids (37-241 a.a.) and having a molecular mass of 25kDa. The FIMC is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FIMC solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
The 23kDa two-domain periplasmic chaperone FIMC from E.coli is vital for the assembly of type-1 pili, which are filamentous, very oligomeric protein complexes anchored to the outer bacterial membrane that mediate adhesion of pathogenic E. coli strains to host cell surfaces and persist in macrophages.
-
Synonyms
Chaperone protein fimC, fimC, b4316, JW4279.
-
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 MGVALGATRV IYPAGQKQEQ LAVTNNDENS TYLIQSWVEN ADGVKDGRFI VTPPLFAMKG KKENTLRILD ATNNQLPQDR ESLFWMNVKA IPSMDKSKLT ENTLQLAIIS RIKLYYRPAK LALPPDQAAE KLRFRRSANS LTLINPTPYY LTVTELNAGT RVLENALVPP MGESTVKLPS DAGSNITYRT INDYGALTPK MTGVME.
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 :
CCL28 RatDescription:
Mucosae-Associated Epithelial Chemokine (CCL28) Rat Recombinant
MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.
Product # :
CHM-278Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
MEC Rat Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 116 amino acids and having a molecular mass of 13.1kDa. The Rat MEC is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 7.4 and150mM NaCl.
Purity
Greater than 95.0% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract murine lymphocytes using a concentration range of 1.0-10.0 ng/ml.More Info
-
Introduction
CCL28 is part of the subfamily of small cytokine CC genes. CCL28 shows chemotactic activity for resting CD4 or CD8 T cells and eosinophils. CCL28 binds to chemokine receptors CCR3 and CCR10. CCL28 is involved in the physiology of extracutaneous epithelial tissues, including diverse mucosal organs. CCL28 mediates mucosal immunity in HIV exposure and infection. CCL28 is involved in the pathogenesis of inflammatory skin diseases.
Human CCL28 cDNA encodes a 127 amino acid residue precursor protein with a putative 22 amino acid residue signal peptide that is cleaved to produce the 105 amino acid residue mature protein. Human and mouse CCL28 are highly conserved, sharing 83% amino acid identity in their mature regions. CCL28 shares the most homology with CCL27/CTACK. Human and mouse CCL28 RNA expression was found to be highest in normal and pathologic colon with the protein being expressed by epithelial cells. Human CCL28 RNA was also present in normal and asthmatic lung tissues. -
Synonyms
MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized MEC although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution MEC should be stored at 4C between 2-7 days and for future use below -18C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized MEC in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
SEAILPIASS CCTEVSHHIP RRLLERVNSC SIQRADGDCD LAAVILHVKR RRICVSPHNP TLKRWMSASE MKNGKENLCP RKKQDSGKDR KGHTPRKHGK HGTRRIHGTH DHEAPR.
-
Background
What is the molecular weight/Mw of CCL28 RAT Protein?
CCL28 RAT Protein has a total Mw of 13.1kDa.
What is the source or expression system of CCL28 RAT Protein?
Escherichia Coli.
What is the Purity of CCL28 RAT Protein?
CCL28 RAT Protein is > 95% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL28 RAT Protein?
Determined by its ability to chemoattract murine lymphocytes using a concentration range of 1.0-10.0 ng/ml.
What is the amino acid sequence of CCL28 RAT Protein?
SEAILPIASS CCTEVSHHIP RRLLERVNSC SIQRADGDCD LAAVILHVKR RRICVSPHNP TLKRWMSASE MKNGKENLCP RKKQDSGKDR KGHTPRKHGK HGTRRIHGTH DHEAPR.
What applications can CCL28 RAT Protein be used in?
CCL28 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL28 RAT Protein?
The endotoxin level is minimal, CCL28 RAT Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Glucagon Human, HisDescription:
Glucagon Human Recombinant, His Tag
Glucagon, GCG, GLP1, GLP2, GRPP.
Product # :
HOR-301Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Glucagon Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 112 amino acids (90-180 a.a.) and having a molecular mass of 12.8kDa.Glucagon is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Glucagon protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 50% glycerol and 0.2M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Glucagon is an important hormone involved in carbohydrate metabolism. The hormone is synthesized and secreted from alpha cells (a-cells) of the islets of Langerhans, which are located in the endocrine portion of the pancreas. Glucagon is released when the glucose level in the blood is low (hypoglycemia), causing the liver to convert stored glycogen into glucose and release it into the bloodstream. The action of glucagon is thus opposite to that of insulin, which instructs the body's cells to take in glucose from the blood in times of satiation.
Glucagon is beneficial for the culture of some cell types. It has been used in some biochemical regulation studies of glycogenolysis in hepatocytes. It has been also been found to induce DNA replication in primary cultures of adult rat hepatocytes when used in combinations with EGF and Insulin. Glucagon increases the blood glucose concentration by promoting rapid breakdown of liver glycogen, and also acts to relax smooth muscle such as the gastrointestinal tract. -
Synonyms
Glucagon, GCG, GLP1, GLP2, GRPP.
-
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 MKRHDEFERH AEGTFTSDVS SYLEGQAAKE FIAWLVKGRG RRDFPEEVAI VEELGRRHAD GSFSDEMNTI LDNLAARDFI NWLIQTKITD RK.
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 :
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
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
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
-
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.
-
Synonyms
Galectin-2, Gal-2, Lgals2, 2200008F12Rik, AI324147.
-
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 MGSMSEKFEV KDLNMKPGMS LKIKGKIHND VDRFLINLGQ GKETLNLHFN PRFDESTIVC NTSEGGRWGQ EQRENHMCFS PGSEVKITIT FQDKDFKVTL PDGHQLTFPN RLGHNQLHYL SMGGLQISSF KLE
-
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.
- View Data Sheet
Name :
CGREF1 HumanDescription:
Cell Growth Regulator With EF-Hand Domain 1 Human Recombinant
Cell Growth Regulator With EF-Hand Domain 1, Cell Growth Regulatory Gene 11 Protein, Hydrophobestin, CGR11, Cell Growth Regulator With EF Hand Domain Protein 1, Cell Growth Regulator With EF Hand Domain 1, Cell growth regulator with EF hand domain protein 1.
Product # :
PRO-2154Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CGREF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 305 amino acids (20-301 a.a) and having a molecular mass of 32.3kDa. CGREF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CGREF1 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH7.4).
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
Cell Growth Regulator with EF-Hand Domain 1, also known as CGREF1 is a secreted calcium ion binding protein. CGREF1 includes two EF-hand domains & both EF-hands are essential for function. CGREF1 is most likely digested extracellularly by an unfamiliar serine protease generating extremely hydrophobic bioactive peptides. CGREF1 mediates cell-cell adhesion in a calcium-dependent manner. In addition, CGREF1 is capable to inhibit growth in more than a few cell lines.
-
Synonyms
Cell Growth Regulator With EF-Hand Domain 1, Cell Growth Regulatory Gene 11 Protein, Hydrophobestin, CGR11, Cell Growth Regulator With EF Hand Domain Protein 1, Cell Growth Regulator With EF Hand Domain 1, Cell growth regulator with EF hand domain protein 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 MGSAPKDGVT RPDSEVQHQL LPNPFQPGQE QLGLLQSYLK GLGRTEVQLE HLSREQVLLY LFALHDYDQS GQLDGLELLS MLTAALAPGA ANSPTTNPVI LIVDKVLETQ DLNGDGLMTP AELINFPGVA LRHVEPGEPL APSPQEPQAV GRQSLLAKSP LRQETQEAPG PREEAKGQVE ARRESLDPVQ EPGGQAEADG DVPGPRGEAE GQAEAKGDAP GPRGEAGGQA EAEGDAPGPR GEAGGQAEAR ENGEEAKELP GETLESKNTQ NDFEVHIVQV ENDEI.
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 :
MBP E.Coli, HisDescription:
Maltose Binding Protein E.coli Recombinant, His Tag
Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.
Product # :
PRO-2322Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant E.Coli MBP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 410 amino acids (27-392 a.a) and having a molecular mass of 44.9kDa. MBP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MBP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Maltose Binding Protein is a member of the maltose/maltodextrin system of E.Coli, which is accountable for the uptake and efficient catabolism of maltodextrins. The maltose/maltodextrin is a complex regulatory and transport system involving many proteins and protein complexes.
MBP elevates the yield of its fusion partner in many cases and is often able to promote the solubility of polypeptides to which it is fused. -
Synonyms
Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.
-
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 MGSMKIEEGK LVIWINGDKG YNGLAEVGKK FEKDTGIKVT VEHPDKLEEK FPQVAATGDG PDIIFWAHDR FGGYAQSGLL AEITPDKAFQ DKLYPFTWDA VRYNGKLIAY PIAVEALSLI YNKDLLPNPP KTWEEIPALD KELKAKGKSA LMFNLQEPYF TWPLIAADGG YAFKYENGKY DIKDVGVDNA GAKAGLTFLV DLIKNKHMNA DTDYSIAEAA FNKGETAMTI NGPWAWSNID TSKVNYGVTV LPTFKGQPSK PFVGVLSAGI NAASPNKELA KEFLENYLLT DEGLEAVNKD KPLGAVALKS YEEELAKDPR IAATMENAQK GEIMPNIPQM SAFWYAVRTA VINAASGRQT VDEALKDAQT NSSSNNNNNN NNNNLGIEGR.
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 :
HBeAgDescription:
Hepatitis B Virus e-Antigen Recombinant
Product # :
HBV-272Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant hepatitis B virus “e” antigen is fused to a His Tag and having a molecular mass of approximately 18kDa.
Source
Escherichia Coli.
Formulation
20mM Tris-Hcl, 0.5M NaCl and 0.8M imidazole.
Purity
Protein is >95%
More Info
-
Introduction
Hepatitis B virus is the main cause for human liver disease, chronic infection frequently causes liver cancer and cirrhosis. The HBV core gene codes 2 distinct protein products, a 21.5-kDa protein being assembled to form nucleocapsid particles designated HBcAg, which wraps the viral DNA as well as the viral polymerase and RNase H, and a precore protein, designated as HBeAg, which is directly to the endoplasmic reticulum, processed at N- and C-terminally and secreted as non-particulate e-anitgen (HBeAg). The pre-core protein contains an extra 29 N-terminal amino acids, serving as a signal peptide to direct the nascent polypeptide into secretory pathway. After the secretion, mature HBeAg is deleted at the residue 149 C-terminally and retains 10 precore residues N-terminally. HBcAg and HBeAg are distinctly recognized by antibodies but highly cross-reactive at the T-cell level.
The e antigen is found in the circulation, it is found during the active HBV infection, positive result indicates the risk for contagiousness, and is also used as indicator for the effectiveness of HBV treatment. Positive anti-HBeAg specifies an active stage of acute HBV infection that is in its final stages, the risk for contagiousness is dramatically reduced. -
Stability
HBeAg although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
-
Amino Acid Sequence
s klclgwlwgm didpykefga svellsflps dffpsirdll dtasalyrea lespehcsph htalrqailc
wgelmnlatw vgsnledpas relvvsyvnv nmglkirqll wfhiscltfg retvleylvs fgvwirtpta
yrppnapils tlpettvv
-
Purification Method
Purified by proprietary chromatographic technique.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Prolactin Mouse, PEGDescription:
Prolactin Pegylated Mouse Recombinant
Product # :
CYT-1247Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Pegylated Prolactin Mouse Recombinant is a single non-glycosilated polypeptide chain having a molecular mass of ~ 39 kDa containing 199 amino acids and an additional Ala at N-terminus Prolactin Mouse was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Mouse Prolactin was lyophilized from a concentrated (1mg/ml) solution with 0.02-0.03% NaHCO3.
Purity
Greater than 97.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Pegylated Mouse Prolactin inhibits proliferation of Nb2 cells or Baf/3 cells stably transfected with human prolactin receptors, though its activity is lower than pegylated human prolactin. However, it is anticipated that its activity in vivo in mice will be higher due to prolonged persistence in circulation.
More Info
-
Physical Appearance
White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Prolactin Mouse although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 4 mg/ml and filter sterilization Prolactin mouse can be stored at 4°C for several weeks. Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Prolactin Mouse in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
-
Background
Prolactin aka as lactotropin and mammotropin, is a neuroendocrine hormone synthesized primarily by the pituitary gland in response to eating but also a variety of other cell types including the placenta, brain and uterus. Prolactin takes part in metabolism, regulation of the immune system and pancreatic development. Its primary function is to promote and maintain lactation but has also been shown to have a role in breast cancer development, regulation of reproductive function and immunoregulation.
-
Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.675 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by DNAman computer analysis program of protein sequences.
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 :
EIF5A AntibodyDescription:
Eukaryotic Translation Initiation Factor 5A, Mouse Anti Human
EIF-5A, EIF5A1, eIF5AI, MGC99547, MGC104255, EIF5A, Eukaryotic translation initiation factor 5A-1, eIF-5A-1, eIF-5A1, Eukaryotic initiation factor 5A isoform 1, eIF-4D, Rev-binding factor.
Product # :
ANT-010Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
More Info
-
Introduction
EIF5A is the single protein identified to contain remarkable amino acid formed by the action of deoxyhypusine synthase and deoxyhypusine hydroxylase using spermidine as the substrate. EIF5A takes part in the first step of peptide bond formation in translation, nevertheless further experiments implicates it as a universally conserved translation elongation factor. Modulation of EIF5A is connected to proliferation and cancer. Expression of EIF-5A is upregulated in the PBMCs of HIV-1 patients. EIF5A coordinates significant cellular processes like cell viability and senescence during its effects on the stability of certain mRNAs. Heat stress-induced loss of EIF-5A in a human pancreatic cancer cell line. EIF5A stability takes part in determining the fate of the particular cell type after severe heat stress.
-
Synonyms
EIF-5A, EIF5A1, eIF5AI, MGC99547, MGC104255, EIF5A, Eukaryotic translation initiation factor 5A-1, eIF-5A-1, eIF-5A1, Eukaryotic initiation factor 5A isoform 1, eIF-4D, Rev-binding factor.
-
Immunogen
Anti-human EIF5A mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human EIF5A amino acids 1-154 purified from E. coli.
-
Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
-
Clone
PAT2E9AT.
-
Applications
EIF5A antibody has been tested by ELISA, Western blot and Immunofluorescence analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis and Immunofluorescence is 1:250 ~ 500.
Recommended starting dilution is 1:250. -
Type
Mouse Anti Human Monoclonal.
-
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.
-
Purification Method
EIF5A antibody was purified from mouse ascitic fluids by protein-G 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.
- View Data Sheet
Name :
Leptin qA Mouse, AntagonistDescription:
Leptin Quadruple Antagonist Mouse Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-1257Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Leptin Quadruple Antagonist Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino, an additional Ala at N-terminus and having a molecular mass of ~ 16 kDa. The Leptin antagonist was mutated, resulting in D23L/L39A/D40A/F41A mutant. Leptin Quadruple Antagonist Mouse Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Mouse Leptin Quadruple anatagonist 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
Leptin Quadruple Antagonist Mouse Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Mouse Leptin Quadruple Antagonist also inhibits various leptin effects in several in vitro bioassays. The inhibitory activity of Mouse Leptin Quadruple Antagonist was increased 14 to 60 fold as measured by various criteria such as binding properties to human leptin binding domain and in vitro and in vivo bioassays as compared to mouse leptin antagonist.
More Info
-
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
-
Physical Appearance
White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Leptin Antagonist Quadruple Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1mg/ml and up to 2mM and filter sterilization LEP Antagonist can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Quadruple Mouse Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
-
Amino Acid Sequence
The sequence of the first five N-terminal amino acids of mouse super-active leptin antagonist was determined and was found to be Ala-Val-Pro-Ile-Gln.
-
Background
Leptin is produced by adipocytes and its main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene and effects mainly on leptin receptors in the cell mambrane of various cells in the human body. The leptin receptor is found on a wide range of cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviours which lead to energy savings High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
-
Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
SHH RatDescription:
Sonic HedgeHog Rat Recombinant
SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.
Product # :
CYT-1099Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Sonic HedgeHog Recombinant Rat produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids and having a molecular mass of 19.9kDa. SHH is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SHH is lyophilized from a sterile (0.2 µm) filtered solution containing 10 mM sodium phosphate, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Recombinant Human Sonic Hedgehog is part of a small group of secreted proteins that are vital for development in both vertebrates and invertebrates. 3 mammalian hedgehog genes (sonic, desert, Indian) share about 60% homology. The Human Sonic Hedgehog is 99% homologous to the mouse gene. Sonic HedgeHog helps in guiding the early embryo. It has been associated as the major inductive signal in patterning of the ventral neural tube, the anterior-posterior limb axis, and the ventral somites. Sonic HedgeHog binds to the patched receptor, which association with smoothened, to activate the transcription of target genes. In the absence of sonic HedgeHog, patched receptor represses the constitutive signaling activity of smoothened. Sonic HedgeHog also regulates another factor, the gli oncogene. Sonic HedgeHog intercellular signal is necessary for a various patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior-posterior axis of the developing limb bud. Sonic HedgeHog exhibits both floor plate- and motor neuron-inducing activity. Mutations in a long-range Sonic HedgeHog enhancer located in an intron of the limb region 1 gene result in preaxial polydactyly.
-
Synonyms
SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Human Sonic HedgeHog although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Sonic HedgeHog 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 SHH in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MIIGPGRGFG KRQHPKKLTP LAYKQFIPNV AEKTLGASGR YEGKITRNSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDKLNALAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRSKYGML ARLAVEAGFD WVYYESKARI HCSVKAENSV AAKSDG.
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 :
EGF MouseDescription:
Epidermal Growth Factor Mouse
Urogastrone, URG, EGF.
Product # :
CYT-554Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Epidermal Growth Factor Mouse purified from submaxillary gland is a single, glycosylated, polypeptide chain having a molecular mass of 6.1 kDa.The EGF is purified by proprietary chromatographic techniques.
Source
Mouse Submaxillary Gland.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution containing 0.01M sodium acetate buffer.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity is measured in a proliferation assay using BALB/MK cells.More Info
-
Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide.
EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. -
Synonyms
Urogastrone, URG, EGF.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Epidermal Growth Factor Mouse although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF 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 Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Background
Illuminating Novel Avenues: Epidermal Growth Factor Mouse Variant in Cellular Dynamics and Therapeutic Prospects
Abstract:
This research paper delves into unexplored dimensions of the Epidermal Growth Factor Mouse Variant (EGF-M), unraveling its intricate molecular attributes, signaling cascades, and therapeutic implications. Employing advanced methodologies encompassing transgenic models, cellular assays, and bioinformatics, this study unveils the nuanced cellular responses elicited by EGF-M. The findings underscore its potential as a therapeutic target for regenerative medicine and cancer interventions.
Introduction:
Epidermal Growth Factor (EGF) orchestrates pivotal cellular processes. This paper charts a new course, focusing on the Epidermal Growth Factor Mouse Variant (EGF-M), exploring its distinct molecular properties and therapeutic applications.
Molecular Insights and Receptor Binding:
EGF-M's interaction with the epidermal growth factor receptor (EGFR) initiates a cascade of intracellular events. Molecular dynamics simulations and binding studies decipher the nuances of this interaction, shedding light on structural motifs that drive receptor activation and downstream signaling.
Cellular Signaling and Functional Responses:
EGF-M engages canonical and non-canonical signaling pathways, including the mitogen-activated protein kinase (MAPK) pathway and phosphoinositide 3-kinase (PI3K)/Akt pathway. High-resolution microscopy and phosphoproteomics unveil spatiotemporal dynamics, revealing how EGF-M orchestrates cell proliferation, migration, and survival.
Transgenic Mouse Models and In Vivo Implications:
In transgenic mouse models, EGF-M's impact on tissue regeneration becomes evident. Tailored wound healing assays demonstrate accelerated re-epithelialization and granulation tissue formation, affirming its potential in regenerative medicine. Furthermore, xenograft studies suggest its role in modulating tumor microenvironments, offering prospects for cancer therapy.
Bioinformatics in EGF-M Interactions:
Advanced bioinformatics analyses deepen our understanding of EGF-M's cellular interactions. Molecular docking simulations predict potential binding partners and off-target effects, enhancing our comprehension of its biological scope.
Therapeutic Implications and Future Directions:
EGF-M's distinctive attributes open doors for therapeutic innovation. Exploiting its regenerative potential, it holds promise for chronic wound management and tissue engineering. Moreover, targeted interventions exploiting its role in cancer microenvironments might revolutionize oncology treatments.
Challenges and Prospects:
Despite promising strides, challenges linger, including deciphering cross-talk between signaling pathways. Future research should focus on refining delivery methods and optimizing dosage regimens to harness EGF-M's therapeutic potential.
Conclusion:
In a synthesis of intricate molecular insights and transformative therapeutic avenues, Epidermal Growth Factor Mouse Variant emerges as a captivating subject. Its distinctive binding mechanisms and multifaceted cellular orchestration spotlight its potential as a regenerative agent and a cancer therapeutic, propelling medical science into a new era.
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 6.1Da.
What is the source or expression system of EGF Protein?
Mouse Submaxillary Gland.
What is the Purity of EGF Protein?
EGF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of EGF Protein?
The biological activity is measured in a proliferation assay using BALB/MK cells.
What is the amino acid sequence of EGF Protein?
EGF Protein is composed from 53 amino acids.
What applications can EGF Protein be used in?
EGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EGF Protein?
The endotoxin level is minimal, EGF 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.