Search results
1000 results found for “Pleiotrophin”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
CPSF4 HumanDescription:
Cleavage And Polyadenylation Specific Factor 4 Human Recombinant
CPSF30, NAR, NEB1, Neb-1, CPSF 30 kDa subunit, NS1 effector domain-binding protein 1.
Product # :
PRO-1406Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CPSF4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 267 amino acids (1-244 a.a.) and having a molecular mass of 29.9kDa.CPSF4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CPSF4 protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
Cleavage And Polyadenylation Specific Factor 4 (CPSF4) is a member of the CPSF4/YTH1 family. CPSF4 complex plays a vital role in pre-mRNA 3'-end formation, distinguishing the AAUAAA signal sequence and interacting with poly(A) polymerase and further factors to bring about cleavage and poly(A) additive. CPSF4 binds RNA polymers with a preference for poly(U).
-
Synonyms
CPSF30, NAR, NEB1, Neb-1, CPSF 30 kDa subunit, NS1 effector domain-binding protein 1.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMQEIIAS VDHIKFDLEI AVEQQLGAQP LPFPGMDKSG AAVCEFFLKA ACGKGGMCPF RHISGEKTVV CKHWLRGLCK KGDQCEFLHE YDMTKMPECY FYSKFGECSN KECPFLHIDP ESKIKDCPWY DRGFCKHGPL CRHRHTRRVI CVNYLVGFCP EGPSCKFMHP RFELPMGTTE QPPLPQQTQP PAKQRTPQVI GVMQSQNSSA GNRGPRPLEQ VTCYKCGEKG HYANRCTKGH LAFLSGQ.
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 :
VEGF Rat, YeastDescription:
Vascular Endothelial Growth Factor Rat Recombinant, Yeast
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Product # :
CYT-1126Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Vascular Endothelial Growth Factor Rat Recombinant produced in yeast is a disulfide-linked homodimer consisting of 2x165 amino acid polypeptide chains, having a molecular mass of approximately 25.7kDa each.VEGF is purified by proprietary chromatographic techniques.
Source
Saccharomyces cerevisiae
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The ED50 was measured in a cell proliferation assay using HUVEC human umbilical vein endothelial cells and was found to be 0.75‑3.75 ng/ml.
More Info
-
Introduction
Vascular endothelial growth factor is an important signaling protein involved in both angiogenesis and vasculogenesis.VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of VEGF is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in VEGF have been associated with proliferative and nonproliferative diabetic retinopathy. -
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized VEGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Vascular Endothelial Growth Factor 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 Vascular Endothelial Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MAPTTEGEQK AHEVVKFMDV YQRSYCRPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCAGC CNDEALECVP TSESNVTMQI MRIKPHQSQH IGEMSFLQHS RCECRPKKDR TKPEKHCEPC SERRKHLFVQ DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR.
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 :
POU5F1 Human, PolyRDescription:
POU Class 5 Homeobox 1 Human Recombinant, Polyarginine-Tag
POU domain class 5 transcription factor 1, Octamer-binding protein 3, Oct-3, Octamer-binding protein 4, Oct-4, Octamer-binding transcription factor 3, OTF-3, POU5F1, OCT3, OCT4, OTF3, OTF4, MGC22487.
Product # :
PRO-091Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
POU5F1 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 360 amino acids and having a molecular mass of 38.6kDa.The POU5F1 is fused to a C-terminal poly-arginine tag and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
POU5F1 0.2µm filtered solution in PBS, pH7.4 and 5% glycerol.
Purity
Greater than 95.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
POU5F1 is a homeodomain transcription factor of the POU family, expressed in embryonic stem (ES) cells and embryonic carcinoma (EC) cells.POU5F1 is significantly involved in the signaling pathway for maintaining self-renewal and pluripotency of ES cells. POU5F1 has 2 distinct DNA binding domains which independently bind half-sites of the canonical octamer motif. This flexibility allows POU5F1 to bind with distinct DNA motifs by forming heterodimers with other transcription factors or by forming homodimers in several conformations. Human POU5F1 contains a 75aa POU specific (POUS) domain and a 60aa POU-Homeo-(POUH) domain connected by a linker region. The Human POU5F1 specifically interacts with Octamer motif ATGCAAAT. In addition, 2 proline-rich domains in the N-terminal and C-terminal regions are vital for POU5F1 transactivation. POU5F1 regulates a number of target genes and has been shown to work jointly with other transcription factors including Sox2 as well as Nanog to sustain stem cell potency and self-renewal.
-
Synonyms
POU domain class 5 transcription factor 1, Octamer-binding protein 3, Oct-3, Octamer-binding protein 4, Oct-4, Octamer-binding transcription factor 3, OTF-3, POU5F1, OCT3, OCT4, OTF3, OTF4, MGC22487.
-
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.Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Gly-His-Leu.
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 :
GDF5 MouseDescription:
Growth and Differentiation factor 5 Mouse Recombinant
Bmp-14, Bp, GDF-5, Bone morphogenetic protein 14, GDF5, Growth/differentiation factor 5.
Product # :
CYT-941Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
GDF5 Mouse Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 120 amino acids and having a molecular mass of 27.2kDa.The GDF-5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GDF-5 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.
Purity
Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 1.0µg/ml, corresponding to a specific activity of > 1000IU/mg.More Info
-
Introduction
GDF-5 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. Mutations in this gene are associated with acromesomelic dysplasia, Hunter-Thompson type; brachydactyly, type C; and chondrodysplasia, Grebe type. These associations confirm that the gene product plays a role in skeletal development.
-
Synonyms
Bmp-14, Bp, GDF-5, Bone morphogenetic protein 14, GDF5, Growth/differentiation factor 5.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized GDF5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF-5 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized GDF5 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
APLANRQGKR PSKNLKARCS RKALHVNFKD MGWDDWIIAP LEYEAFHCEG LCEFPLRSHL EPTNHAVIQT LMNSMDPEST PPTCCVPTRL SPISILFIDS ANNVVYKQYE DMVVESCGCR.
-
Background
What is the molecular weight/Mw of GDF5 MOUSE Protein?
GDF5 MOUSE Protein has a total Mw of 27.2kDa.
What is the source or expression system of GDF5 MOUSE Protein?
Escherichia Coli.
What is the Purity of GDF5 MOUSE Protein?
GDF5 MOUSE Protein is >96% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF5 MOUSE Protein?
The ED50 as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 1.0µg/ml, corresponding to a specific activity of > 1000IU/mg.
What is the amino acid sequence of GDF5 MOUSE Protein?
APLANRQGKR PSKNLKARCS RKALHVNFKD MGWDDWIIAP LEYEAFHCEG LCEFPLRSHL EPTNHAVIQT LMNSMDPEST PPTCCVPTRL SPISILFIDS ANNVVYKQYE DMVVESCGCR.
What applications can GDF5 MOUSE Protein be used in?
GDF5 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF5 MOUSE Protein?
The endotoxin level is minimal, GDF5 MOUSE 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 :
ANXA5 HumanDescription:
Annexin A5 Human Recombinant
PP4, ANX5, ENX2, ANXA5, Annexin A5, Annexin-5, Annexin V, Lipocortin V, Endonexin II, Calphobindin I, CBP-I, Placental anticoagulant protein I, PAP-I, Placental anticoagulant protein 4, Thromboplastin inhibitor, Vascular anticoagulant-alpha, VAC-alpha, Anchorin CII.
Product # :
PRO-732Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
ANXA5 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 320 amino acids (1-320 a.a.) and having a molecular mass of 35.9 kDa.ANXA5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ANXA5 protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
ANXA5 is a member of the annexin family of calcium-dependent phospholipid binding proteins which are involved in membrane-related activity along exocytotic and endocytotic pathways. ANXA5 is a phospholipase A2 and protein kinase C inhibitory protein with calcium channel properties and takes part in cellular signal transduction, inflammation, growth and differentiation. ANXA5 is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. ANXA5 regulates coagulability in the blood stream by binding to phosphatidylserine and sulfatide. ANXA5 protects sinsuoidal endothelial cells from ischemia reperfusion damage. ANXA5 is necessary for normal CFTR chloride channel activity.
-
Synonyms
PP4, ANX5, ENX2, ANXA5, Annexin A5, Annexin-5, Annexin V, Lipocortin V, Endonexin II, Calphobindin I, CBP-I, Placental anticoagulant protein I, PAP-I, Placental anticoagulant protein 4, Thromboplastin inhibitor, Vascular anticoagulant-alpha, VAC-alpha, Anchorin CII.
-
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
MAQVLRGTVT DFPGFDERAD AETLRKAMKG LGTDEESILT LLTSRSNAQR QEISAAFKTL FGRDLLDDLK SELTGKFEKL IVALMKPSRL YDAYELKHAL KGAGTNEKVL TEIIASRTPE ELRAIKQVYE EEYGSSLEDD VVGDTSGYYQ RMLVVLLQAN RDPDAGIDEA QVEQDAQALF QAGELKWGTD EEKFITIFGT RSVSHLRKVF DKYMTISGFQ IEETIDRETS GNLEQLLLAV VKSIRSIPAY LAETLYYAMK GAGTDDHTLI RVMVSRSEID LFNIRKEFRK NFATSLYSMI KGDTSGDYKK ALLLLCGEDD.
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 :
Streptavidin (37-159), HisDescription:
Streptavidin (37-159 a.a) Recombinant, His Tag
Product # :
PRO-1495Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Streptavidin Recombinant produced in E. coli is a single polypeptide chain containing 148 amino acids (37-159) and having a molecular mass of 15.6kDa. Streptavidin is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The Streptavidin solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is widely used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.
-
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 MGSHMAEAGI TGTWYNQLGS TFIVTAGADG ALTGTYESAV GNAESRYVLT GRYDSAPATD GSGTALGWTV AWKNNYRNAH SATTWSGQYV GGAEARINTQ WLLTSGTTEA NAWKSTLVGH DTFTKVKP.
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 :
BRAF HumanDescription:
B-Raf Proto-Oncogene Human Recombinant
Proto-Oncogene B-Raf, BRAF1, RAFB1, NS7, EC 2.7.11.1, B-RAF1, P94.
Product # :
PKA-071Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
BRAF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 360 amino acids (432-766a.a) and having a molecular mass of 40.6kDa. BRAF is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BRAF protein solution (0.25mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
-
Introduction
B-Raf Proto-Oncogene, also known as BRAF is a member of the raf/mil family of serine/threonine protein kinases. BRAF participates in regulating the MAP kinase/ERKs signaling pathway, which eventually have an effect on cell division, differentiation, and secretion. Mutations in BRAF have been associated with cardiofaciocutaneous syndrome, which is a disease characterized by heart defects, mental retardation and a distinctive facial appearance. In addition, mutations in BRAF have also been associated with different cancers, including non-Hodgkin lymphoma, colorectal cancer, malignant melanoma, thyroid carcinoma, non-small cell lung carcinoma, as well as adenocarcinoma of lung.
-
Synonyms
Proto-Oncogene B-Raf, BRAF1, RAFB1, NS7, EC 2.7.11.1, B-RAF1, P94.
-
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 MGSEFSEDRN RMKTLGRRDS SDDWEIPDGQ ITVGQRIGSG SFGTVYKGKW HGDVAVKMLN VTAPTPQQLQ AFKNEVGVLR KTRHVNILLF MGYSTKPQLA IVTQWCEGSS LYHHLHIIET KFEMIKLIDI ARQTAQGMDY LHAKSIIHRD LKSNNIFLHE DLTVKIGDFG LATVKSRWSG SHQFEQLSGS ILWMAPEVIR MQDKNPYSFQ SDVYAFGIVL YELMTGQLPY SNINNRDQII FMVGRGYLSP DLSKVRSNCP KAMKRLMAEC LKKKRDERPL FPQILASIEL LARSLPKIHR SASEPSLNRA GFQTEDFSLY ACASPKTPIQ AGGYGAFPVH.
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 :
C8G HumanDescription:
Complement Component 8, Gamma Human Recombinant
Complement component 8 gamma polypeptide, C8C, complement component C8 gamma chain, MGC142186.
Product # :
PRO-947Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
C8G Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 203 amino acids (21-202) and having a molecular mass of 22.6 kDa.The C8G is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The C8G solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.15M NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
C8, a component of the complement system consists of three polypeptides C8A, C8B and C8G and takes part in the formation of Membrane Attack Complex (MAC). Patients with C8 deficiency are exposed to several bacteria infections. C8G, a member of the lipocalin family and calycin superfamily, is a secreted protein that can bind retinol. C8G is created in the liver, monocytes and fibroblast and has a role in clearing pathogens from an infected host.
-
Synonyms
Complement component 8 gamma polypeptide, C8C, complement component C8 gamma chain, MGC142186.
-
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 MQKPQRPRRP ASPISTIQPK ANFDAQQFAG TWLLVAVGSA CRFLQEQGHR AEATTLHVAP QGTAMAVSTF RKLDGICWQV RQLYGDTGVL GRFLLQARGA RGAVHVVVAE TDYQSFAVLY LERAGQLSVK LYARSLPVSD SVLSGFEQRV QEAHLTEDQI FYFPKYGFCE AADQFHVLDE VRR
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 :
TMEFF1 HumanDescription:
TMEFF1 Human Recombinant
C9orf2, CT120.1, H7365, TR-1, Tomoregulin-1, Transmembrane protein with EGF-like and one follistatin-like domain, TMEFF1.
Product # :
PRO-1429Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
TMEFF1 Human Recombinant produced in E. coli is a single polypeptide chain containing 314 amino acids (40-330) and having a molecular mass of 33.9kDa. TMEFF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TMEFF1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
TMEFF1 is a type I transmembrane glycoprotein which includes 2 follistatin modules and an EGF domain in its extracellular domain, a transmembrane domain and a short cytoplasmic tail. The extracellular domain of TMEFF1 can be released as a soluble protein. TMEFF1 is primarily expressed in brain, but is downregulated in brain neoplasms. TMEFF1 selectively regulates nodal but not activin signaling through direct binding to the nodal co-receptor, Cripto. TMEFF inhibits NODAL and BMP signaling through neural patterning and also a possible tumor suppressor in brain cancers.
-
Synonyms
C9orf2, CT120.1, H7365, TR-1, Tomoregulin-1, Transmembrane protein with EGF-like and one follistatin-like domain, TMEFF1.
-
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 MGSSNQPPGG GGGSGGDCPG GKGKSINCSE LNVRESDVRV CDESSCKYGG VCKEDGDGLK CACQFQCHTN YIPVCGSNGD TYQNECFLRR AACKHQKEIT VIARGPCYSD NGSGSGEGEE EGSGAEVHRK HSKCGPCKYK AECDEDAENV GCVCNIDCSG YSFNPVCASD GSSYNNPCFV REASCIKQEQ IDIRHLGHCT DTDDTSLLGK KDDGLQYRPD VKDASDQRED VYIGNHMPCP ENLNGYCIHG KCEFIYSTQK ASCRCESGYT GQHCEKTDFS ILYVVPSRQK LTHV.
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 :
KRT17 HumanDescription:
Cytokeratin 17 Human Recombinant
Keratin 17, PCHC1, 39.1, CK-17, K17, PC2, PC, cytokeratin-17, Keratin 17 Epitope S1, Keratin 17 Epitope S2, Keratin 17 Epitope S4, Keratin, Type I Cytoskeletal 1, keratin-17, Cytokeratin-17, Keratin-17.
Product # :
PRO-1883Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
KRT17 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 455 amino acids (1-432 a.a) and having a molecular mass of 50.5kDa.KRT17 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
KRT17 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
Cytokeratin 17 also known as KRT17 is a type I cytokeratin. KRT17 is found in nail beds, hair follicles, sebaceous glands, and other epidermal appendages. Mutations in KRT17 lead to Jackson-Lawler type pachyonychia congenita and steatocystoma multiplex. KRT17 takes part in the formation and maintenance of a variety of skin appendages, particularly in determining shape and orientation of hair. KRT17 also modulates the function of TNF-alpha in the precise context of hair cycling. Moreover, KRT17 regulates protein synthesis and epithelial cell growth all through binding to the adapter protein SFN and by stimulating Akt/mTOR pathway.
-
Synonyms
Keratin 17, PCHC1, 39.1, CK-17, K17, PC2, PC, cytokeratin-17, Keratin 17 Epitope S1, Keratin 17 Epitope S2, Keratin 17 Epitope S4, Keratin, Type I Cytoskeletal 1, keratin-17, Cytokeratin-17, Keratin-17.
-
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).Please avoid freeze thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMTTSIRQ FTSSSSIKGS SGLGGGSSRT SCRLSGGLGA GSCRLGSAGG LGSTLGGSSY SSCYSFGSGG GYGSSFGGVD GLLAGGEKAT MQNLNDRLAS YLDKVRALEE ANTELEVKIR DWYQRQAPGP ARDYSQYYRT IEELQNKILT ATVDNANILL QIDNARLAAD DFRTKFETEQ ALRLSVEADI NGLRRVLDEL TLARADLEMQ IENLKEELAY LKKNHEEEMN ALRGQVGGEI NVEMDAAPGV DLSRILNEMR DQYEKMAEKN RKDAEDWFFS KTEELNREVA TNSELVQSGK SEISELRRTM QALEIELQSQ LSMKASLEGN LAETENRYCV QLSQIQGLIG SVEEQLAQLR CEMEQQNQEY KILLDVKTRL EQEIATYRRL LEGEDAHLTQ YKKEPVTTRQ VRTIVEEVQD GKVISSREQV HQTTR
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 :
ARTN HumanDescription:
Artemin Human Recombinant
ART, ARTN , EVN, NBN.
Product # :
CYT-306Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Artemin Human Recombinant produced in E.Coli is a disulfide-linked homodimer, non-glycosylated, polypeptide chain containing 2 x 113 amino acids and having a total molecular mass of 24.2 kDa. Artemin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Artemin was lyophilized after extensive dialysis against 10mM sodium citrate pH-4.5 and 25mM sodium chloride.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity is determined by the dose-dependent proliferation of the SH-SY5Y cell line and is typically 4-8 ng/mL. The activity can also be determined by its ability to promote survival and neurite outgrowth.More Info
-
Introduction
The protein encoded by this gene is a member of the glial cell line-derived neurotophic factor (GDNF) family of ligands which are a group of ligands within the TGF-beta superfamily of signaling molecules. GDNFs are unique in having neurotrophic properties and have potential use for gene therapy in neurodegenrative disease. Artemin has been shown in culture to support the survival of a number of periferal neuron populations and at least one population of dopaminergic CNS neurons. Its role in the PNS and CNS is further substantiated by its expression pattern in the proximity of these neurons. This protein is a ligand for the RET receptor and uses GFR-alpha 3 as a coreceptor. Four alternatively spliced transcripts have been described, two of which encode the same protein.
-
Synonyms
ART, ARTN , EVN, NBN.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Artemin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Artemin Human Recombinant 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 Artemin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
AGGPGSRARA AGARGCRLRS QLVPVRALGL GHRSDELVRF RFCSGSCRRA RSPHDLSLAS LLGAGALRPP PGSRPVSQPC CRPTRYEAVS FMDVNSTWRT VDRLSATACG CLG.
-
Background
Artemin Human Recombinant: Unraveling its Role in Neurobiology and Therapeutic Applications
Abstract:
Artemin, a member of the glial cell line-derived neurotrophic factor (GDNF) family, holds significant potential in neurobiology and therapeutic interventions. This research paper provides an overview of Artemin human recombinant, elucidating its molecular characteristics, signaling pathways, and therapeutic implications in neurological disorders. Understanding the multifaceted role of Artemin offers new avenues for targeted therapies. This article offers a concise analysis of Artemin, highlighting its impact on neurobiology and its therapeutic applications.
Introduction:
Neurological disorders represent a major challenge in healthcare, necessitating innovative therapeutic strategies. Artemin, a member of the GDNF family, has emerged as a promising molecule in neurobiology. This paper provides an overview of Artemin, shedding light on its structure, function, and therapeutic potential.
Artemin Signaling and Mechanisms:
Artemin binds to its receptor, Ret tyrosine kinase, and activates downstream signaling pathways, including the PI3K/AKT and MAPK pathways. These signaling cascades play crucial roles in neuronal survival, growth, and differentiation, highlighting the significance of Artemin in neurodevelopment and neuroprotection.
Artemin in Neurological Disorders:
Artemin has been implicated in various neurological disorders, including peripheral neuropathies and neurodegenerative diseases. Its neuroprotective properties and ability to enhance neuronal survival and regeneration make it a promising target for therapeutic interventions. Furthermore, Artemin may play a role in pain modulation and sensory neuron function.
Therapeutic Potential of Artemin Human Recombinant:
Artemin human recombinant offers promising prospects in the field of neurotherapeutics. Strategies aimed at modulating Artemin signaling or delivering exogenous Artemin hold potential for promoting neuronal survival, regeneration, and functional recovery. Artemin-based therapies could be developed for a range of neurological disorders, including peripheral neuropathies, Parkinson's disease, and spinal cord injuries.
Challenges and Future Directions:
While the therapeutic targeting of Artemin shows promise, several challenges lie ahead. Further research is needed to understand the precise mechanisms underlying Artemin's effects and its interactions with other signaling pathways. Additionally, the development of effective delivery methods and the identification of patient subgroups that may benefit from Artemin-based therapies are important considerations for clinical translation.
Conclusion:
Artemin human recombinant represents a promising avenue for therapeutic interventions in neurological disorders. Understanding the molecular mechanisms and functional implications of Artemin in neurobiology offers new opportunities for developing innovative treatments. Continued research in this field has the potential to improve the lives of individuals affected by neurological conditions and advance the field of neurotherapeutics.
What is the molecular weight/Mw of ARTN Protein?
ARTN Protein has a total Mw of 24.2kDa.
What is the source or expression system of ARTN Protein?
Escherichia Coli.
What is the Purity of ARTN Protein?
ARTN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of ARTN Protein?
The activity is determined by the dose-dependent proliferation of the SH-SY5Y cell line and is typically 4-8 ng/mL. The activity can also be determined by its ability to promote survival and neurite outgrowth.
What is the amino acid sequence of ARTN Protein?
AGGPGSRARA AGARGCRLRS QLVPVRALGL GHRSDELVRF RFCSGSCRRA RSPHDLSLAS LLGAGALRPP PGSRPVSQPC CRPTRYEAVS FMDVNSTWRT VDRLSATACG CLG.
What applications can ARTN Protein be used in?
ARTN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ARTN Protein?
The endotoxin level is minimal, ARTN 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 :
VEGF AntibodyDescription:
Vascular Endothelial Cell Growth Factor, Mouse Anti-Human
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Product # :
ANT-125Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- More Info
More Info
-
Introduction
Vascular endothelial growth factoris an important signaling proteininvolved in both vasculogenesisand angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of this protein is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy. -
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
-
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
-
Immunogen
r.HumanVEGF.
-
Ig Subclass
Mouse IgM.
-
Clone
NYRhVEGF.
-
Applications
Direct ELISA, Western Blot, Immuneprecipitation.
-
Titer
By direct ELISA, 1:10,000 dilution will yield 0.15 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
-
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
-
Type
Mouse Anti Human Monoclonal.
-
Storage Procedures
In lyophilized form, for long periods, store at 4oC in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.
-
Purification Method
Boric acid precipitation Protein concentration1mg/ml in PBS (after reconstitution).
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 :
NELFE HumanDescription:
Negative Elongation Factor Complex Member E Human Recombinant
Negative elongation factor E, NELF-E, RNA-binding protein RD, NELFE, RD, RDBP, Negative Elongation Factor Complex Member E, D6S45, RDP.
Product # :
PRO-1968Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
NELFE Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 403 amino acids (1-380) and having a molecular mass of 45.6 kDa.NELFE is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The NELFE solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 5mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
NELFE is a vital component of NELF complex which represses RNA polymerase II transcript elongation. NELFE is similar to nuclear RNA-binding proteins but does not bind RNA. NELFE contains a tract of alternating basic and acidic residues, mainly arginine and aspartic acid.
-
Synonyms
Negative elongation factor E, NELF-E, RNA-binding protein RD, NELFE, RD, RDBP, Negative Elongation Factor Complex Member E, D6S45, RDP.
-
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 MGSMLVIPPG LSEEEEALQK KFNKLKKKKK ALLALKKQSS SSTTSQGGVK RSLSEQPVMD TATATEQAKQ LVKSGAISAI KAETKNSGFK RSRTLEGKLK DPEKGPVPTF QPFQRSISAD DDLQESSRRP QRKSLYESFV SSSDRLRELG PDGEEAEGPG AGDGPPRSFD WGYEERSGAH SSASPPRSRS RDRSHERNRD RDRDRERDRD RDRDRDRERD RDRDRDRDRD RERDRDRERD RDRDREGPFR RSDSFPERRA PRKGNTLYVY GEDMTPTLLR GAFSPFGNII DLSMDPPRNC AFVTYEKMES ADQAVAELNG TQVESVQLKV NIARKQPMLD AATGKSVWGS LAVQNSPKGC HRDKRTQIVY SDDVYKENLV DGF.
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 Human His CDescription:
Macrophage Migration Inhibitory Factor Human Recombinant, His Tag C-Terminus
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
Product # :
CYT-521Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
MIF human Recombinant, fused to His-tag at C-terminus, was cloned into an E. coli expression vector and was purified to apparent homogeneity by using conventional column chromatography techniques.Macrophage Inducing Factor Human Recombinant is a single, non-glycosylated, polypeptide chaincontaining 123 amino acidsand having a molecular mass of 13.5 kDa.
Source
Escherichia Coli.
Formulation
Human MIF was lyophilized from a 1mg/ml solution containing PBS pH-7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Measured by its ability to bind rhCD74 in a functional ELISA.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 lyophilized powder.
-
Stability
Lyophilized MIF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIF 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 MIF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MPMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLMAFGGSSEPC
ALCSLHSIGKIGGAQNRSYSKLLCGLLAERLRISPDRVYINYYDMNAANVGWNNSTF
ALEHHHHHH.
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 :
Secretin HumanDescription:
Secretin Human
Product # :
HOR-273Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- formulation
- purity
- More Info
Description
Secretin has a molecular formula of C130H220N44O41, a.a. sequence of H-His-Ser-Asp-Gly-Thr-Phe-Thr-Ser-Glu-Leu-Ser-Arg-Leu-Arg- Asp-Ser-Ala-Arg-Leu-Gln-Arg-Leu-Leu-Gln-Gly-Leu-Val-NH2 and having an Mw of 3055.4 Dalton.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
Human Secretin stimulates the secretion of bicarbonate by the pancreas and inhibits the production of gastrin and acid production in the stomach. It also potentiates the release of digestive enzymes from the pancreas triggered by cholecystokinin.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Secretin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Secretin 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 Secretin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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 :
IL 3 RatDescription:
Interleukin-3 Rat Recombinant
MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.
Product # :
CYT-383Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Interleukin-3 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 144 amino acids and having a molecular mass of 16.3kDa. The IL-3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Interleukin-3 Rat was 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 as determined by the dose-dependent stimulation of the proliferation of thymidine uptake by murine MC-9 cells is < 10 ng/ml, corresponding to a specific activity of >1.0 x 105 units/mg.More Info
-
Introduction
Interleukin-3 is a pleiotropic cytokine produced primarily by activated T cells.
IL-3 is thought to function via specific cell surface receptors to stimulate the proliferation, differentiation and survival of haematopoietic cell lines. IL-3 has also been shown to affect the functional activity of a variety of other cell types including mast cells, eosinophils, megakaryocytes and basophils. -
Synonyms
MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Interleukin-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL3 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 Interleukin 3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MISDRGSDAH HLLRTLDCRT IALEILVKLP YPQVSGLNNS DDKANLRNST LRRVNLDEFL KSQEEFDSQD TTDIKSKLQK LKCCIPAAAS DSVLPGVYNK DLDDFKKKLR FYVIHLKDLQ PVSVSRPPQP TSSSDNFRPM TVEC.
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 :
GMFB MouseDescription:
Glia Maturation Factor Beta Mouse Recombinant
Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF, C79176, AI851627, D14Ertd630e, 3110001H22Rik, 3110001O16Rik.
Product # :
CYT-006Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Glia Maturation Factor-Beta (GMF-Beta) Mouse Recombinant produced in E.Coli is a signle, non-glycosylated, polypeptide chain containing 141 amino acids and having a total molecular mass of 16.6kDa. GMF-Beta, Mouse Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GMF-beta protein was 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.More Info
-
Introduction
GMFB is part of the GMF subfamily of the larger actin-binding protein ADF family. GMFB is phosphorylated after phorbol ester stimulation, and is crucial for the nervous system. GMFB causes brain cell differentiation, stimulates neural regeneration and inhibits tumor cell proliferation. GMFB overexpression in astrocytes results in the increase of BDNF production. GMFB expression is increased by exercise, thus BDNF is important for exercise-induction of BDNF.
-
Synonyms
Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF, C79176, AI851627, D14Ertd630e, 3110001H22Rik, 3110001O16Rik.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized GMF-B although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMF-beta 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 GMFB in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
SESLVVCDVA EDLVEKLRKF RFRKETHNAA IIMKIDKDER LVVLDEELEG
VSPDELKDEL PERQPRFIVY SYKYQHDDGR VSYPLCFIFS SPVGCKPEQQ
MMYAGSKNKL VQTAELTKVF EIRNTEDLTE EWLREKLGFF H. -
Background
What is the molecular weight/Mw of GMFB MOUSE Protein?
GMFB MOUSE Protein has a total Mw of 16.6kDa.
What is the source or expression system of GMFB MOUSE Protein?
Escherichia Coli.
What is the Purity of GMFB MOUSE Protein?
GMFB MOUSE Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of GMFB MOUSE Protein?
The biological functionality of GMFB MOUSE Protein will be determined in the future.
What is the amino acid sequence of GMFB MOUSE Protein?
SESLVVCDVA EDLVEKLRKF RFRKETHNAA IIMKIDKDER LVVLDEELEG
VSPDELKDEL PERQPRFIVY SYKYQHDDGR VSYPLCFIFS SPVGCKPEQQ
MMYAGSKNKL VQTAELTKVF EIRNTEDLTE EWLREKLGFF H.
What applications can GMFB MOUSE Protein be used in?
GMFB MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GMFB MOUSE Protein?
The endotoxin level is minimal, GMFB MOUSE 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 :
IGFBP 5 HumanDescription:
Insulin-Like Growth Factor Binding Protein-5 Human Recombinant
IGFBP-5, IBP-5, IGF-binding protein 5.
Product # :
CYT-464Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
IGFBP5 Human Recombinant produced in E.Coli is non-glycosylated homodimer containing 2x252 amino acids and having a molecular mass of 28.6kDa. IGFBP5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IBP-5 was lyophilized from a concentrated (1mg/ml) solution containing 10mM sodium Citrate pH-3.
Purity
Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50, calculated by its ability to inhibit IGF-II induced proliferation of MCF-7. The expected ED50 for this effect is < 0.4µg/ml, corresponding to a specific activity of > 2500 IU/mg in the presence of 15ng/ml of rHuIGF-II.More Info
-
Introduction
IGFBP5 is a member of the insulin-like growth factor binding protein (IGFBP) family and encodes a protein with an IGFBP domain and a thyroglobulin type-I domain. The protein forms a ternary complex with insulin-like growth factor acid-labile subunit (IGFALS) and either insulin-like growth factor (IGF) I or II. In this form, it circulates in the plasma, prolonging the half-life of IGFs and altering their interaction with cell surface receptors. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
-
Synonyms
IGFBP-5, IBP-5, IGF-binding protein 5.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized IBP5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGFBP 5 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Insulin-Like Growth Factor Binding Protein-5 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
LGSFVHCEPC DEKALSMCPP SPLGCELVKE PGCGCCMTCA LAEGQSCGVY TERCAQGLRC LPRQDEEKPL HALLHGRGVC LNEKSYREQV KIERDSREHE EPTTSEMAEE TYSPKIFRPK HTRISELKAE AVKKDRRKKL TQSKFVGGAE NTAHPRIISA PEMRQESEQG PCRRHMEASL QELKASPRMV PRAVYLPNCD RKGFYKRKQC KPSRGRKRGI CWCVDKYGMK LPGMEYVDGD FQCHTFDSSN VE.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
OSTF1 HumanDescription:
Osteoclast Stimulating Factor-1 Human Recombinant
SH3P2, OSF, OSTF-1, Osteoclast-stimulating factor 1, OSTF1, FLJ20559, bA235O14.1.
Product # :
CYT-630Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
OSTF1 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 225 amino acids (1-217) and having a molecular mass of 25.1kDa. The OSTF1 is fused to an 8 amino acid His Tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
OSTF1 protein (1mg/ml) solution contains 20mM Tris-HCl buffer pH 8, 0.5mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
OSTF1 is an intracellular protein produced by osteoclasts that induces bone resorption, via signaling cascade which results in the secretion of factors enhancing osteoclast formation and activity.
-
Synonyms
SH3P2, OSF, OSTF-1, Osteoclast-stimulating factor 1, OSTF1, FLJ20559, bA235O14.1.
-
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).Please avoid freeze thaw cycles.
-
Amino Acid Sequence
MSKPPPKPVK PGEGGQVKVF RALYTFEPRT PDELYFEEGD IIYITDMSDT NWWKGTSKGR TGLIPSNYVA EQAESIDNPL HEAAKRGNLS WLRECLDNRV GVNGLDKAGS TALYWACHGG HKDIVEMLFT QPNIELNQQN KLGDTALHAA AWKGYADIVQ LFLAKGARTD LRNIEKKLAF DMATNAACAS LLKKKQGTDA VRTLSNAEDY LDDEDSDLEH HHHHH.
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 :
TNFR2 HumanDescription:
Tumor Necrosis Factor Receptor Type 2 Human Recombinant
Tumor necrosis factor receptor superfamily member 1B, Tumor necrosis factor receptor 2, TNF-R2, Tumor necrosis factor receptor type II, TNF-RII, TNFR-II, p75, p80 TNF-alpha receptor, TNFRSF1B, TNFBR, TNFR2.
Product # :
CYT-769Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
TNFR2 Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 184 amino acids and having a molecular mass of 20kDa. The TNFR2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TNFR2 was Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by its ability to inhibit the TNF-a mediated cytotoxicity in the L-929 cells is less than 0.2µg/ml, corresponding to a specific activity of > 5000IU/mg in the presence of 0.25ng/mL of rHuTNF-a.More Info
-
Introduction
TNFR2 belongs to the TNF-receptor superfamily. TNFR2 is receptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. TNFR2 mediates the majority of the metabolic effects of TNF-alpha. In addition, knockout studies in mice propose a role for TNFR2 in protecting neurons from apoptosis by stimulating antioxidative pathways. TNFR2 expression might have a significant role in the angiogenesis, tumor cell proliferation and metastasis of Invasive micropapillary carcinoma of the breast.
There are 2 types of soluble TNF receptors: sTNFR-I and sTNFR-II, which act to neutralize the biological activities of TNF alpha and TNF beta. The levels of these soluble receptors seem to increase as a result of shedding of the extracellular domains of the membrane bound receptors. High levels of soluble TNF receptors are found in the amniotic fluid of pregnant women. TNFR2 and TNFR1 form a heterocomplex which mediates the recruitment of 2 anti-apoptotic proteins, c-IAP1 and c-IAP2, which possess E3 ubiquitin ligase activity. IAPs’ function in TNF-receptor signaling is unknown; nevertheless, c-IAP1 is believed to potentiate TNF-induced apoptosis by the ubiquitination and degradation of TNF-receptor-associated factor 2, which mediates anti-apoptotic signals. Oxidative stress promotes TNFR1 and TNFR2 self-interaction, ligand-independent and enhanced ligand-dependent TNF signaling. TNF-a, TNFR1 and TNFR2 have roles in cellular differentiation. TNFR1 and TNFR2 function in cell type-specific renal injury. -
Synonyms
Tumor necrosis factor receptor superfamily member 1B, Tumor necrosis factor receptor 2, TNF-R2, Tumor necrosis factor receptor type II, TNF-RII, TNFR-II, p75, p80 TNF-alpha receptor, TNFRSF1B, TNFBR, TNFR2.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized TNFR2 although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution TNFR2 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 TNFR2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MPAQVAFTPY APEPGSTCRL REYYDQTAQM CCSKCSPGQH AKVFCTKTSD TVCDSCEDST YTQLWNWVPE CLSCGSRCSS DQVETQACTR EQNRICTCRP GWYCALSKQE GCRLCAPLRK CRPGFGVARP GTETSDVVCK PCAPGTFSNT TSSTDICRPH QICNVVAIPG NASMDAVCTS TSPT.
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 :
IL 9 MouseDescription:
Interleukin-9 Mouse Recombinant
P40, HP40, T-cell growth factor p40, IL-9, P40 cytokine.
Product # :
CYT-373Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Interleukin-9 Mouse Recombinant produced in E.Coli is a single, non-glycosylated single polypeptide chain containing 127 amino acids and having a molecular mass of 14.3kDa. The IL-9 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution 10mM Na2PO4, pH 7.5.
Purity
Greater than 96.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by the dose-dependant stimulation of human MO7e cells is < 0.5 ng/ml, corresponding to a Specific Activity of 2,000,000IU/mg.More Info
-
Introduction
Factor that is thought to be a regulator of hematopoiesis. It has been shown to enhance the growth of human mast cells and megakaryoblastic leukemic cells as well as murine helper t-cell clones. IL-9 is a glycoprotein with a molecular weight of 32-39 that is derived from T-cells, and maps to human chromosome 5.
-
Synonyms
P40, HP40, T-cell growth factor p40, IL-9, P40 cytokine.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Interleukin-9 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL9 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 Interleukin 9 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MQRCSTTWGI RDTNYLIENL KDDPPSKCSC SGNVTSCLCL SVPTDDCTTP CYREGLLQLT NATQKSRLLP VFHRVKRIVE VLKNITCPSF SCEKPCNQTM AGNTMSFLKS LLGTFQKTEM QRQKSRP.
-
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.6 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-9 as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TGF b AntibodyDescription:
Transforming Growth Factor-beta, Mouse-Anti Human
Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.
Product # :
ANT-168Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- formulation
- More Info
Formulation
1mg/ml in PBS (after reconstitution).
More Info
-
Introduction
Transforming growth factor betas (TGFBetas) mediate many cell-cell interactions that occur during embryonic development. Three TGFBetas have been identified in mammals. TGFBeta1, TGFBeta2 and TGFBeta3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule. This antibody reacts with the precursor and mature form of TGFBeta2 and to a lesser extent TGFBeta3, but does not cross react with TGFBeta1.
-
Synonyms
Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.
-
Solubility
Reconstitute with 0.5ml H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
-
Immunogen
r.Human TGF-b.
-
Ig Subclass
Mouse IgG1.
-
Clone
hTGF-b.
-
Note
This antibody will bind very well to protein A in a buffer (PBS) containing high salt concentration (3M Nacl).
-
Titer
In direct ELISA, using alkaline phosphatase goat anti-mouse Ig (Jackson ImmunoResearch Laboratories) 1:10,000 dilution will yield 0.7 O.D within 10 minutes.
-
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
-
Type
Mouse Anti Human Monoclonal.
-
Storage Procedures
Lyophilized: store at 4oC. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.
-
Purification Method
Ion exchange column.
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 :
IGFBP 1 HumanDescription:
Insulin-Like Growth Factor Binding Protein-1 Human Recombinant
IBP-1, IGF-Binding Protein 1, AFBP, PP12, IGF-BP25, hIGFBP-1, IGFBP-1.
Product # :
CYT-299Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
IGFBP-1 Human Recombinant (26-259 a.a.) produced in NS0 is a single, glycosylated, polypeptide chain containing 234 amino acids and having a molecular mass of 25kDa. The IGFBP1 is purified by proprietary chromatographic techniques.
Source
Mouse myeloma cell line, NS0.
Formulation
IGFBP-1 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as determined by the inhibition of rHuIGF-I-induced proliferation of human MCF-7 cells, is less than 4µg/ml.More Info
-
Introduction
IGFBP1 is a member of the insulin-like growth factor binding protein (IGFBP) family and encodes a protein with an IGFBP domain and a thyroglobulin type-I domain. The protein binds both insulin-like growth factors (IGFs) I and II and circulates in the plasma. Binding of this protein prolongs the half-life of the IGFs and alters their interaction with cell surface receptors. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
-
Synonyms
IBP-1, IGF-Binding Protein 1, AFBP, PP12, IGF-BP25, hIGFBP-1, IGFBP-1.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized IGFBP1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF-BP1 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 IBP-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
APWQCAPCSA EKLALCPPVS ASCSEVTRSA GCGCCPMCAL PLGAACGVAT ARCARGLSCR ALPGEQQPLH ALTRGQGACV QESDASAPHA AEAGSPESPE STEITEEELL DNFHLMAPSE EDHSILWDAI STYDGSKALH VTNIKKWKEP CRIELYRVVE SLAKAQETSG EEISKFYLPN CNKNGFYHSR QCETSMDGEA GLCWCVYPWN GKRIPGSPEI RGDPNCQIYF NVQN.
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 :
Follistatin HumanDescription:
Follistatin Human Recombinant
FST, FS
Product # :
CYT-232Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Follistatin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 288 amino acids and having a total molecular mass of 31.5kDa.The FST is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing no additives.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity is determined by the ability to neutralize ACTV inhibitory effect of mouse MPC-11 cells. The expected ED50 is 100-400ng/ml, corresponding to a Specific Activity of 2,500-10,000units/mg in the presence of 7.5ng/ml ACTV A.
More Info
-
Introduction
Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA. In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin. Follistatin functions as an ACTV antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).
-
Synonyms
FST, FS
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Follistatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FST 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 Follistatin in sterile 18MΩ-cm H2O 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 Gly-Asn-Cys-Trp-Leu.
-
Background
What is the molecular weight/Mw of FOLLISTATIN HUMAN Protein?
FOLLISTATIN HUMAN Protein has a total Mw of 31.5kDa.
What is the source or expression system of FOLLISTATIN HUMAN Protein?
Escherichia Coli.
What is the Purity of FOLLISTATIN HUMAN Protein?
FOLLISTATIN HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FOLLISTATIN HUMAN Protein?
The activity is determined by the ability to neutralize ACTV inhibitory effect of mouse MPC-11 cells. The expected ED50 is 100-400ng/ml, corresponding to a Specific Activity of 2,500-10,000units/mg in the presence of 7.5ng/ml ACTV A.
What is the amino acid sequence of FOLLISTATIN HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Asn-Cys-Trp-Leu.
What applications can FOLLISTATIN HUMAN Protein be used in?
FOLLISTATIN HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FOLLISTATIN HUMAN Protein?
The endotoxin level is minimal, FOLLISTATIN 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.