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Description:

Prefoldin Subunit 2 Human Recombinant

Prefoldin subunit 2, PFDN2, PFD2.

Product # :

PRO-001

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Description

PFDN2 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 174 amino acids (1-154 a.a.) and having a molecular mass of 18.8kDa. The PFDN2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PFDN2 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 1mM DTT and 50mM NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Prefoldin subunit 2 (PFDN2) belongs to the prefoldin beta subunit family. The PFDN2 protein is one of 6 subunits of prefoldin, which is a molecular chaperone complex that binds and stabilizes newly synthesized polypeptides, thus allowing them to fold correctly. PFDN2 binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. PFDN2 also binds to a nascent polypeptide chain and promotes folding in an setting in which there are many competing pathways for nonnative proteins.
Synonyms
Prefoldin subunit 2, PFDN2, PFD2.
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 MAENSGRAGK SSGSGAGKGA VSAEQVIAGF NRLRQEQRGL ASKAAELEME LNEHSLVIDT LKEVDETRKC YRMVGGVLVE RTVKEVLPAL ENNKEQIQKI IETLTQQLQA KGKELNEFRE KHNIRLMGED EKPAAKENSE GAGAKASSAG VLVS.

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

Description:

Peptidase Inhibitor 3 Human Recombinant, Sf9

Elafin, ESI, SKALP, WAP3, WFDC14.

Product # :

PRO-2653

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Description

PI3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 101 amino acids (23-117a.a) and having a molecular mass of 10.7kDa.PI3 is fused to an 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The PI3 solution (0.2mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Peptidase Inhibitor 3, also referred to PI3, is neutrophil and pancreatic elastase-specific inhibitor of skin. The protein may prevent elastase mediated tissue proteolysis. PI3 has shown inhibition of alpha-4-beta-2/CHRNA2-CHRNB2 nicotinic acetylcholine receptor, a weak inhibition on Kv11.1/KCNH2/ERG1 and on the transient receptor potential cation channel subfamily V member 1.
Synonyms
Elafin, ESI, SKALP, WAP3, WFDC14.
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
AVTGVPVKGQ DTVKGRVPFN GQDPVKGQVS VKGQDKVKAQ EPVKGPVSTK PGSCPIILIR CAMLNPPNRC LKDTDCPGIK KCCEGSCGMA CFVPQHHHHH H

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

Description:

Complement Factor B Human Recombinant, Sf9

CFB, AHUS4, ARMD14, BF, BFD, CFAB, CFBD, FB, FBI12, GBG, H2-Bf, PBF2, Complement Factor B, B-Factor, Properdin, Properdin Factor B, C3/C5 Convertase, EC 3.4.21.47, PBF2,Glycine-Rich Beta-Glycoprotein, Glycine-Rich Beta Glycoprotein, C3 Proaccelerator, C3 Proactivator , EC 3.4.2, FBI12, H2-Bf.

Product # :

PRO-2403

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Description

CFB Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 245 amino acids (26-259a.a.) and having a molecular mass of 27.3kDa (Molecular size on SDS-PAGE will appear at approximately 28-40 kDa). CFB is expressed with a 11 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Complement Factor B, also known as CFB, encodes complement factor B which is a component of the alternative pathway of complement activation. Factor B circulates in the blood as a single chain polypeptide. Once the alternative pathway is activated it is cleaved by complement factor D yielding the noncatalytic chain Ba and the catalytic subunit Bb. The active subunit Bb is a serine protease which connects with C3b to form the alternative pathway C3 convertase. Also, Bb is involved in the proliferation of preactivated B lymphocytes, while Ba inhibits their proliferation.
Synonyms
CFB, AHUS4, ARMD14, BF, BFD, CFAB, CFBD, FB, FBI12, GBG, H2-Bf, PBF2, Complement Factor B, B-Factor, Properdin, Properdin Factor B, C3/C5 Convertase, EC 3.4.21.47, PBF2,Glycine-Rich Beta-Glycoprotein, Glycine-Rich Beta Glycoprotein, C3 Proaccelerator, C3 Proactivator , EC 3.4.2, FBI12, H2-Bf.
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
ADPEFTPWSL ARPQGSCSLE GVEIKGGSFR LLQEGQALEY VCPSGFYPYP VQTRTCRSTG SWSTLKTQDQ KTVRKAECRA IHCPRPHDFE NGEYWPRSPY YNVSDEISFH CYDGYTLRGS ANRTCQVNGR WSGQTAICDN GAGYCSNPGI PIGTRKVGSQ YRLEDSVTYH CSRGLTLRGS QRRTCQEGGS WSGTEPSCQD SFMYDTPQEV AEAFLSSLTE TIEGVDAEDG HGPGEQQKRH 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.

Description:

MAK16 Human Recombinant

Protein MAK16 homolog, NNP78, Protein RBM13, RBM13, MAK16L, RBM13.

Product # :

PRO-2086

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Description

MAK16 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (1-300 a.a) and having a molecular mass of 37.8kDa (Molecular size on SDS-PAGE will appear higher).MAK16 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MAK16 protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
MAK16 is a member of the MAK16 family.
Synonyms
Protein MAK16 homolog, NNP78, Protein RBM13, RBM13, MAK16L, RBM13.
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 MGSMQSDDVI WDTLGNKQFC SFKIRTKTQS FCRNEYSLTG LCNRSSCPLA NSQYATIKEE KGQCYLYMKV IERAAFPRRL WERVRLSKNY EKALEQIDEN LIYWPRFIRH KCKQRFTKIT QYLIRIRKLT LKRQRKLVPL SKKVERREKR REEKALIAAQ LDNAIEKELL ERLKQDTYGD IYNFPIHAFD KALEQQEAES DSSDTEEKDD DDDDEEDVGK REFVEDGEVD ESDISDFEDM DKLDASSDED QDGKSSSEEE EEKALSAKHK GKMPLRGPLQ RKRAYVEIEY EQETEPVAKA KTT.

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

Description:

Hepatocyte Growth Factor Human Recombinant, HEK

Scatter Factor (SF), Hepatopoietin (HPTA), HGF, HGFB, F-TCF.

Product # :

CYT-090

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Description

HGF Human Recombinant produced in HEK cells is a glycosylated disulfide-linked heterodimer, containing 697 a.a. (Gln-32 to Ser-728) having a total molecular weight of 80kDa. The HGF is purified by proprietary chromatographic techniques.

Source

HEK.

Formulation

The HGF was lyophilized from a solution (1mg/ml) containing 10mM Sodium phosphate, 150mM NaCl, 0.01% Tween 80 and 100mM L-Arginine, pH 6.5.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The activity was measured in a cell proliferation assay using 4MBr-5 rhesus monkey epithelial cells (ATCC CCL-208). The EC₅₀for this effect is typically 20-40ng/ml.

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Introduction
Hepatocyte Growth Factor (HGF) is a multifunctional growth factor which regulates both cell growth and cell motility. It exerts a strong mitogenic effect on hepatocytes and primary epithelial cells. HGF synergizes with Interleukin-3 and GM-CSF to stimulate colony formation of hematopoietic progenitor cells in vitro and may, therefore, also modulate hematopoiesis.
Synonyms
Scatter Factor (SF), Hepatopoietin (HPTA), HGF, HGFB, F-TCF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized HGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HGF 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 Hepatocyte 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
32-QRKRRNTIHE FKKSAKTTLI KIDPALKIKT KKVNTADQCA NRCTRNKGLP FTCKAFVFDK ARKQCLWFPF NSMSSGVKKE FGHEFDLYEN KDYIRNCIIG KGRSYKGTVS ITKSGIKCQP WSSMIPHEHS FLPSSYRGKD LQENYCRNPR GEEGGPWCFT SNPEVRYEVC DIPQCSEVEC MTCNGESYRG LMDHTESGKI CQRWDHQTPH RHKFLPERYP DKGFDDNYCR NPDGQPRPWC YTLDPHTRWE YCAIKTCADN TMNDTDVPLE TTECIQGQGE GYRGTVNTIW NGIPCQRWDS QYPHEHDMTP ENFKCKDLRE NYCRNPDGSE SPWCFTTDPN IRVGYCSQIP NCDMSHGQDC YRGNGKNYMG NLSQTRSGLT CSMWDKNMED LHRHIFWEPD ASKLNENYCR NPDDDAHGPW CYTGNPLIPW DYCPISRCEG DTTPTIVNLD HPVISCAKTK QLRVVNGIPT RTNIGWMVSL RYRNKHICGG SLIKESWVLT ARQCFPSRDL KDYEAWLGIH DVHGRGDEKC KQVLNVSQLV YGPEGSDLVL MKLARPAVLD DFVSTIDLPN YGCTIPEKTS CSVYGWGYTG LINYDGLLRV AHLYIMGNEK CSQHHRGKVT LNESEICAGA EKIGSGPCEG DYGGPLVCEQ HKMRMVLGVI VPGRGCAIPN RPGIFVRVAY YAKWIHKIIL TYKVPQS-728
Background
What is the molecular weight/Mw of HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein has a total Mw of 80kDa.

What is the source or expression system of HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
HEK.
What is the Purity of HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
The activity was measured in a cell proliferation assay using 4MBr-5 rhesus monkey epithelial cells (ATCC CCL-208). The EC50 for this effect is typically 20-40ng/ml.
What is the amino acid sequence of HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
32-QRKRRNTIHE FKKSAKTTLI KIDPALKIKT KKVNTADQCA NRCTRNKGLP FTCKAFVFDK ARKQCLWFPF NSMSSGVKKE FGHEFDLYEN KDYIRNCIIG KGRSYKGTVS ITKSGIKCQP WSSMIPHEHS FLPSSYRGKD LQENYCRNPR GEEGGPWCFT SNPEVRYEVC DIPQCSEVEC MTCNGESYRG LMDHTESGKI CQRWDHQTPH RHKFLPERYP DKGFDDNYCR NPDGQPRPWC YTLDPHTRWE YCAIKTCADN TMNDTDVPLE TTECIQGQGE GYRGTVNTIW NGIPCQRWDS QYPHEHDMTP ENFKCKDLRE NYCRNPDGSE SPWCFTTDPN IRVGYCSQIP NCDMSHGQDC YRGNGKNYMG NLSQTRSGLT CSMWDKNMED LHRHIFWEPD ASKLNENYCR NPDDDAHGPW CYTGNPLIPW DYCPISRCEG DTTPTIVNLD HPVISCAKTK QLRVVNGIPT RTNIGWMVSL RYRNKHICGG SLIKESWVLT ARQCFPSRDL KDYEAWLGIH DVHGRGDEKC KQVLNVSQLV YGPEGSDLVL MKLARPAVLD DFVSTIDLPN YGCTIPEKTS CSVYGWGYTG LINYDGLLRV AHLYIMGNEK CSQHHRGKVT LNESEICAGA EKIGSGPCEG DYGGPLVCEQ HKMRMVLGVI VPGRGCAIPN RPGIFVRVAY YAKWIHKIIL TYKVPQS-728

What applications can HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein be used in?
HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
The endotoxin level is minimal, HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein was purified using conventional chromatography techniques.

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

Description:

Flt3-Ligand Rhesus Macaque Recombinant

Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.

Product # :

CYT-157

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Description

Flt3 Ligand Rhesus Macaque Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 159 amino acids and having a molecular mass of 18.0kDa.The Flt3 Ligand Rhesus Macaque 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 SDS-PAGE.

Biological Activity

The ED50 as calculated by the dose-dependant stimulation of the proliferation of human AML5 cells is less than 1.0ng/ml, corresponding to a specific activity of 1,000,000IU/mg.

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Introduction
FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.
Synonyms
Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Flt3 Ligand Rhesus Macaque although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flt3 Ligand Rhesus Macaque 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 Flt3 Ligand in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
TQDCSFQHSP ISSDFAVKIR ELSDYLLQDY PVTVPSNLQD EELCGALWRL VLAQRWMERL KTVAGSKMQG LLERVNTEIH FVTKCAFQHP PSCLRFVQTN ISRLLQETSE QLVALKPWIT RQNFSRCLEL QCQPDSSTLP PPRSPGALEA TALTAPQRP
Background
What is the molecular weight/Mw of FLT3-LIGAND RHESUS MACAQUE Protein?
FLT3-LIGAND RHESUS MACAQUE Protein has a total Mw of 18kDa.

What is the source or expression system of FLT3-LIGAND RHESUS MACAQUE Protein?
Escherichia Coli.

What is the Purity of FLT3-LIGAND RHESUS MACAQUE Protein?
FLT3-LIGAND RHESUS MACAQUE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of FLT3-LIGAND RHESUS MACAQUE Protein?
The ED50 as calculated by the dose-dependant stimulation of the proliferation of human AML5 cells is less than 1.0ng/ml, corresponding to a specific activity of 1,000,000IU/mg.

What is the amino acid sequence of FLT3-LIGAND RHESUS MACAQUE Protein?
TQDCSFQHSP ISSDFAVKIR ELSDYLLQDY PVTVPSNLQD EELCGALWRL VLAQRWMERL KTVAGSKMQG LLERVNTEIH FVTKCAFQHP PSCLRFVQTN ISRLLQETSE QLVALKPWIT RQNFSRCLEL QCQPDSSTLP PPRSPGALEA TALTAPQRP
What applications can FLT3-LIGAND RHESUS MACAQUE Protein be used in?
FLT3-LIGAND RHESUS MACAQUE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FLT3-LIGAND RHESUS MACAQUE Protein?
The endotoxin level is minimal, FLT3-LIGAND RHESUS MACAQUE Protein was purified using conventional chromatography techniques.

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

Description:

Holo Transferrin Human Recombinant

Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.

Product # :

PRO-2844

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Description

Human Holo Transferrin Recombinant produced in HEK Cells is a glycosylated polypeptide containing 679 amino acids and having a Mw of of 76 kDa.

Source

HEK Cells

Formulation

The protein was lyophilized from 1x PBS pH-7.4.

Purity

Protein is >98% pure as determined by 10% PAGE (coomassie staining).

Biological Activity

The activity of Recombinant Holo Transferrin was determined by the proliferation assay using MDCK cells stimulated with recombinant human Holo Transferrin. The protein was found biologically active

sds-page, activity

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Introduction
Recombinant Human Holo Transferrin is an iron-delivery signaling protein which functions in the delivery of Fe³⁺ iron to cells using transferrin receptor-1 (TfR1/CD71).
Holo-transferrin binds TfR1, undergoes receptor-mediated endocytosis and the iron is released intracellularly. Transferrin Human Recombinant is crucial for brain and the nervous system, neuronal mitochondrial metabolism, neurotransmitter synthesis, oligodendrocyte myelination and synaptic activity. Recombinant holo-transferrin can be used in cell therapy, stem-cell expansion, CHO production, or drug-delivery platforms.
Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.
Physical Appearance
Sterile Filtered lyophilized (freeze-dried) powder.
Stability
Store the lyophilized Holo Transferrin recombinant between 2-8°C, do not freeze.
Upon reconstitution Holo Transferrin 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 Holo Transferrin recombinant in sterile 18MΩ-cm H2O at 1mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VPDKTVRWCA VSEHEATKCQ SFRDHMKSVI PSDGPSVACV KKASYLDCIR AIAANEADAV TLDAGLVYDA YLAPNNLKPV VAEFYGSKED PQTFYYAVAV VKKDSGFQMN QLRGKKSCHT GLGRSAGWNI PIGLLYCDLP EPRKPLEKAV ANFFSGSCAP CADGTDFPQL CQLCPGCGCS TLNQYFGYSG AFKCLKDGAG DVAFVKHSTI FENLANKADR DQYELLCLDN TRKPVDEYKD CHLAQVPSHT VVARSMGGKE DLIWELLNQA QEHFGKDKSK EFQLFSSPHG KDLLFKDSAH GFLKVPPRMD AKMYLGYEYV TAIRNLREGT CPEAPTDECK PVKWCALSHH ERLKCDEWSV NSVGKIECVS AETTEDCIAK IMNGEADAMS LDGGFVYIAG KCGLVPVLAE NYNKSDNCED TPEAGYFAVA VVKKSASDLT WDNLKGKKSC HTAVGRTAGW NIPMGLLYNK INHCRFDEFF SEGCAPGSKK DSSLCKLCMG SGLNLCEPNN KEGYYGYTGA FRCLVEKGDV AFVKHQTVPQ NTGGKNPDPW AKNLNEKDYE LLCLDGTRKP VEEYANCHLA RAPNHAVVTR KDKEACVHKI LRQQQHLFGS NVTDCSGNFC LFRSETKDLL FRDDTVCLAK LHDRNTYEKY LGEEYVKAVG NLRKCSTSSL LEACTFRRP.

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

Description:

Alpha & Gamma-Adaptin Binding Protein Human Recombinant

P34, Alpha- and gamma-adaptin-binding protein p34.

Product # :

PRO-1479

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Description

AAGAB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 335 amino acids (1-315 a.a.) and having a molecular mass of 36.7kDa.AAGAB is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

AAGAB protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Alpha & Gamma-Adaptin Binding Protein (AAGAB), which is also known as P34, takes part in membrane traffic and interacts with AP1G1 and AP2A1.AAGAB is highly expressed in skin and keratinocytes, with the highest levels in adrenal gland, rectum and thymus.
Synonyms
P34, Alpha- and gamma-adaptin-binding protein p34.
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 MAAGVPCALV TSCSSVFSGD QLVQHILGTE DLIVEVTSND AVRFYPWTID NKYYSADINL CVVPNKFLVT AEIAESVQAF VVYFDSTQKS GLDSVSSWLP LAKAWLPEVM ILVCDRVSED GINRQKAQEW CIKHGFELVE LSPEELPEED DDFPESTGVK RIVQALNANV WSNVVMKNDR NQGFSLLNSL TGTNHSIGSA DPCHPEQPHL PAADSTESLS DHRGGASNTT DAQVDSIVDP MLDLDIQELA SLTTGGGDVE NFERLFSKLK EMKDKAATLP HEQRKVHAEK VAKAFWMAIG GDRDEIEGLS SDEEH.

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

Description:

Myeloid/Lymphoid Leukemia Translocated To 11 Human Recombinant

AF1Q, RP11-316M1.10, Protein AF1q, MLLT11.

Product # :

PRO-1991

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Description

MLLT11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 113 amino acids (1-90 a.a) and having a molecular mass of 12.4kDa. MLLT11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MLLT11 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
Myeloid/Lymphoid Leukemia Translocated To 11 (MLLT11) is a part of the Mixed-Lineage Leukemia protein family. MLLT11 which takes part in leukemogenesis and in the progression of severe monocytic leukemia (AML) is located on chromosome 11q23. MLLT11 which is also expressed in embryonic brain cortex is upregulated during neuronal differentiation and is taking part in the evolution of the central nervous system.
Synonyms
AF1Q, RP11-316M1.10, Protein AF1q, MLLT11.
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 MGSMRDPVSS QYSSFLFWRM PIPELDLSEL EGLGLSDTAT YKVKDSSVGK MIGQATAADQ EKNPEGDGLL EYSTFNFWRA PIASIHSFEL DLL.

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

Description:

Surfeit-1 Human Recombinant

SURF1, SURF-1, Surfeit locus protein 1, Surfeit 1.

Product # :

PRO-764

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Description

Surfeit-1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 215 amino acids (80-273 a.a.) and having a molecular mass of 24.3 kDa. The Surfeit-1 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Surfeit-1 solution contains 20 mM Tris-HCl buffer (pH 8.0), 0.1M Nacl, 1mM DTT and 20% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
SURF1 plays a role in the biogenesis of the COX complex. SURF1 is found in the inner mitochondrial membrane and takes part in the biogenesis of the cytochrome c oxidase complex. SURF1 is shares a bidirectional promoter with SURF2 on the opposite strand. Defects in this SURF1 cause Leigh syndrome, a rigorous neurological disorder that is generally associated with systemic cytochrome c oxidase deficiency.
Synonyms
SURF1, SURF-1, Surfeit locus protein 1, Surfeit 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 MQVQRRKWKL NLIAELESRV LAEPVPLPAD PMELKNLEYR PVKVRGCFDH SKELYMMPRT MVDPVREARE GGLISSSTQS GAYVVTPFHC TDLGVTILVN RGFVPRKKVN PETRQKGQIE GEVDLIGMVR LTETRQPFVP ENNPERNHWH YRDLEAMARI TGAEPIFIDA NFQSTVPGGP IGGQTRVTLR NEHLQ.

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

Description:

Programmed Cell Death-5 Human Recombinant

Programmed cell death protein 5, TF-1 cell apoptosis-related protein 19, Protein TFAR19, PDCD5, TFAR19, MGC9294.

Product # :

PRO-624

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Description

PDCD5 Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 125 amino acids and having a molecular mass of 14 kDa.

Source

Escherichia Coli.

Formulation

PDCD5 protein solution contains 1x PBS pH-7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
PDCD5 is expressed in tumor cells during apoptosis independent of the apoptosis-inducing stimuli. Prior to apoptosis induction, PDCD5 is distributed in both the nucleus and cytoplasm. Once apoptosis is induced, the amount of PDCD5 increases and by relocation from the cytoplasm, it accumulates in the nucleus.PDCD5 protein has a stable helical core conformation consisting of a triple-helix bundle and two dissociated terminal regions. PDCD5 is an important novel protein that regulates both apoptotic and non-apoptotic programmed cell death. PDCD5 functions in the process of apoptosis.
PDCD5 plays an important role in regulation of apoptotic processes in gastric cancer cells and gastric tumors.
PDCD5 plays a role in the pathogenesis of rheumatoid arthritis.
-27G/-11A SNP is associated with reduced PDCD5 promoter activity and increased susceptibility to chronic myelogenous leukemia.
PDCD5 gene may be a target gene under the control of some important apoptosis-related transcriptional factors during the cell apoptosis.
Synonyms
Programmed cell death protein 5, TF-1 cell apoptosis-related protein 19, Protein TFAR19, PDCD5, TFAR19, MGC9294.
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
MADEELEALR RQRLAELQAK HGDPGDAAQQ EAKHRGAEMR NSILAQVLDQ SARARLSNLA LVKPEKTKAV ENYLIQMARY GQLSEKVSEQ GLIEILKKVS QQTEKTTTVK LNRRKVMDSD EDDDY.

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

Description:

Fibroblast Growth Factor-18 Rat Recombinant

Fibroblast growth factor 18, FGF-18, zFGF5, Fgf18, D130055P09Rik.

Product # :

CYT-176

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Description

FGF18 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 21.0kDa.The FGF 18 Rat is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2um filtered concentrated solution in PBS and 0.5M NaCl, pH 7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.

Biological Activity

The ED50 as determined by the dose-dependent stimulation of thymidine uptake by BaF3 cells expressing FGF-receptors is < 0.5ng/ml, corresponding to a specific activity of > 2.0×1,000,000 units/mg.

sds-page

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Introduction
Fibroblast growth factor 18 (FGF18) is a member of the large FGF family which has at least 23 members. FGF18 is a growth factor with a core 120 amino acid FGF domain which allows for a common tertiary structure. FGFs are expressed in the course of the embryonic development and in restricted adult tissues. FGF-18 is an indispensable regulator of long bone and calvarial development. FGF-18 signals via FGFR 1c, 2c, 3c, and 4.
Synonyms
Fibroblast growth factor 18, FGF-18, zFGF5, Fgf18, D130055P09Rik.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGF 18 Rat although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF 18 Rat 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 FGF 18 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
EENVDFRIHV ENQTRARDDV SRKQLRLYQL YSRTSGKHIQ VLGRRISARG EDGDKYAQLL VETDTFGSQV RIKGKETEFY LCMNRKGKLV GKPDGTSKEC VFIEKVLENN YTALMSAKYS GWYVGFTKKG RPRKGPKTRE NQQDVHFMKR YPKGQTELQK PFKYTTVTKR SRRIRPTHPG
Background
What is the molecular weight/Mw of FGF18-RAT Protein?
FGF18-RAT Protein has a total Mw of 21kDa.

What is the source or expression system of FGF18-RAT Protein?
Escherichia Coli.

What is the Purity of FGF18-RAT Protein?
FGF18-RAT Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF18-RAT Protein?
The ED50 as determined by the dose-dependent stimulation of thymidine uptake by BaF3 cells expressing FGF-receptors is < 0.5ng/ml, corresponding to a specific activity of > 2.0×1,000,000 units/mg.

What is the amino acid sequence of FGF18-RAT Protein?
EENVDFRIHV ENQTRARDDV SRKQLRLYQL YSRTSGKHIQ VLGRRISARG EDGDKYAQLL VETDTFGSQV RIKGKETEFY LCMNRKGKLV GKPDGTSKEC VFIEKVLENN YTALMSAKYS GWYVGFTKKG RPRKGPKTRE NQQDVHFMKR YPKGQTELQK PFKYTTVTKR SRRIRPTHPG

What applications can FGF18-RAT Protein be used in?
FGF18-RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF18-RAT Protein?
The endotoxin level is minimal, FGF18-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.

Description:

TMEFF1 Human Recombinant

C9orf2, CT120.1, H7365, TR-1, Tomoregulin-1, Transmembrane protein with EGF-like and one follistatin-like domain, TMEFF1.

Product # :

PRO-1429

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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.

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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.

Description:

Adiponectin Globular Recombinant, His Tag

Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

Product # :

CYT-277

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Description

Acrp30 Human has a total of 171 amino acids. N-terminal underlined amino acids are His-tag and the protease cleavage site (31AA-Underlined). The AA sequence of Acrp30 Human is homologous to the 105-244 amino acid sequence of the Human full-length Adiponectin (Swiss-prot entry Q15848).

Source

Escherichia Coli.

Formulation

Acrp30 Human is a filtered powder, lyophilized from 0.6mg/ml in PBS buffer.

Purity

Purity of Acrp30 Human is greater than 95% as determined by SDS PAGE.

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Introduction
Adiponectin is a protein exclusively secreted from adipose tissue. In the circulation, adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (LMW, also called trimer) forms. Different oligomeric complex of adiponectin activates different signaling pathways and exerts distinct functions.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Stability
For long term, store lyophilized Acrp30 Human at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted Acrp30 Human can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C. The lyophilized Acrp30 Human remains stable for 24 months when stored at -20°C.
Solubility
Add deionized water and let the lyophilized pellet of Acrp30 Human dissolve completely.
Amino Acid Sequence
MSWWHHHHHH NWNIPTTQDT TQDLWFEGAM GGEGAYVYRS FSVGLETYV TIPNMPIRFT KIFYNQQNHYDGSTGKFHCN IPGLYYFAYH ITVYMKDVKV SLFKKDKAML FTYDQYQENN VDQASGSVLL HEVGDQVWLQVYGEGERNGL YADNDNDSTF TGFLLYHDTN.
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 16.7kDa.

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

What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >95% pure as determined by SDS-PAGE.

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

What is the amino acid sequence of ADIPONECTIN Protein?
MSWWHHHHHH NWNIPTTQDT TQDLWFEGAM GGEGAYVYRS FSVGLETYV TIPNMPIRFT KIFYNQQNHYDGSTGKFHCN IPGLYYFAYH ITVYMKDVKV SLFKKDKAML FTYDQYQENN VDQASGSVLL HEVGDQVWLQVYGEGERNGL YADNDNDSTF TGFLLYHDTN.

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

What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN Protein was purified using conventional chromatography techniques

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

Description:

Chondrolectin Human Recombinant

Chondrolectin, Transmembrane Protein MT75, C21orf68, Chromosome 21 Open Reading Frame 68, PRED12, MT75, CHODL.

Product # :

PRO-1964

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CHODL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (22-216) and having a molecular mass of 24.6 kDa.CHODL is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Chondrolectin (CHODL) is a type I membrane protein with a carbohydrate recognition domain characteristic of C-type lectins in its extracellular portion. In other proteins, this domain is involved in endocytosis of glycoproteins and exogenous sugar-bearing pathogens. The CHODL protein localizes mainly to the perinuclear region.
Synonyms
Chondrolectin, Transmembrane Protein MT75, C21orf68, Chromosome 21 Open Reading Frame 68, PRED12, MT75, CHODL.
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 MGSFCRRVVS GQKVCFADFK HPCYKMAYFH ELSSRVSFQE ARLACESEGG VLLSLENEAE QKLIESMLQN LTKPGTGISD GDFWIGLWRN GDGQTSGACP DLYQWSDGSN SQYRNWYTDE PSCGSEKCVV MYHQPTANPG LGGPYLYQWN DDRCNMKHNY ICKYEPEINP TAPVEKPYLT NQPGDTHQNV VVTEAGIIPN.

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

Description:

Parathyroid Hormone Related Protein N15 Labeled Human Recombinant

Parathyroid Hormone 2, PTH2, TIPF39, Tuberoinfundibular 39 Residue Protein.

Product # :

HOR-005

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Description

PTHrP N15 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids, having an MW of 10033 Da labeled by the stable isotope N15.The PTHrP is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

PthRp N15 protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS,
pH 7.4.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
PTHrP is a powerful and discriminating agonist of PTH2R which takes part in adenyl cyclase activation and intracellular calcium levels elevation. PTHrP encourages protein kinase C beta activation, recruitment of beta-arrestin and PTH2R internalization. Additionally, PTHrP inhibits cell proliferation through its contribution to PTH2R activation, activates nociceptors and nociceptive circuits and acts as a neuropeptide in spermatogenesis.
Synonyms
Parathyroid Hormone 2, PTH2, TIPF39, Tuberoinfundibular 39 Residue Protein.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized PTHrP N15 although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution PTHrP N15 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 be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10mM HAc to a concentration of 0.1-1.0 mg/mL. Further dilutions should be made in appropriate buffered solutions.
Amino Acid Sequence
AVSEHQLLHD KGKSIQDLRR RFFLHHLIAE IHTAEIRATS EVSPNSKPSP NTKNHPVRFG SDDEGRYLTQ ETNKVETYKE QPLKTP.

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

Description:

Mesencephalic Astrocyte-Derived Neurotrophic Factor Rat Recombinant

Mesencephalic astrocyte-derived neurotrophic factor, Arginine-rich protein, Protein ARMET, Manf, Armet.

Product # :

CYT-828

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Description

MANF Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 158 amino acids and having a molecular mass of 18.2kDa.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by a cell proliferation assay using rat C6 cells is less than 10µg/ml, corresponding to a specific activity of >100 IU/mg.

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Introduction
MANF is a 20kDa protein which belongs to the ARMET family. MANF was originally known as an arginine-rich region protein which was extremely mutated in a large number of tumors. MANF Expression is induced during ER stress, signifying that MANF takes part in protein quality control during ER stress.
Synonyms
Mesencephalic astrocyte-derived neurotrophic factor, Arginine-rich protein, Protein ARMET, Manf, Armet.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MANF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MANF 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 MANF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
LRPGDCEVCI SYLGRFYQDL KDRDVTFSPA TIEEELIKFC REARGKENRL CYYIGATDDA ATKIINEVSK PLAHHIPVEK ICEKLKKKDS QICELKYDKQ IDLSTVDLKK LRVKELKKIL DDWGEMCKGC AEKSDYIRKI NELMPKYAPK AASARTDL.

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

Description:

WAP Four-Disulfide Core Domain 12 Human Recombinant

WAP Four-Disulfide Core Domain 12, Putative Protease Inhibitor WAP12, Whey Acidic Protein 2, Chromosome 20 Open Reading Frame 122, Protease Inhibitor WAP2, Single WAP Motif Protein 2, WAP Four-Disulfide Core Domain Protein 12, dJ211D12.4, C20orf122, SWAM2, WAP2.

Product # :

PRO-1830

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Description

WFDC12 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 111 amino acids (24-111) and having a molecular mass of 12.1 kDa. WFDC12 is fused to a 23 amino acid His-tag at N-terminus.

Source

Escherichia Coli.

Formulation

The WFDC12 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
WFDC12 belongs to the WFDC (WAP-type four-disulfide core) domain family. The WAP signature motif or WFDC domain has four disulfide bonds created by eight cysteines at the core of the protein, which operates as a protease inhibitor.
Synonyms
WAP Four-Disulfide Core Domain 12, Putative Protease Inhibitor WAP12, Whey Acidic Protein 2, Chromosome 20 Open Reading Frame 122, Protease Inhibitor WAP2, Single WAP Motif Protein 2, WAP Four-Disulfide Core Domain Protein 12, dJ211D12.4, C20orf122, SWAM2, WAP2.
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 MGSVKEGIEK AGVCPADNVR CFKSDPPQCH TDQDCLGERK CCYLHCGFKC VIPVKELEEG GNKDEDVSRP YPEPGWEAKC PGSSSTRCPQ K

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

Description:

Cellular Retinoic Acid binding Protein 2 Human Recombinant

RBP6, CRABP-II, CRABP2, RETINOIC ACID-BINDING PROTEIN CELLULAR TYPE II, Cellular retinoic acid-binding protein 2, Cellular retinoic acid-binding protein II.

Product # :

PRO-637

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Description

CRABP2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 136 amino acids and having a molecular mass of 15.6 kDa. The CRABP2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CRABP2 protein solution contains 20mM Tris-HCl pH-8 and 20% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
CRABP2 NCBI Accession No: NP_001869 regulates the access of retinoic acid to the nuclear retinoic acid receptors. CRABP2 is involved in a regulatory feedback mechanism that controls the action of retinoic acid on cell differentiation.
CRABP2 is involved in the conversion of vitamin A into its intracellular active form retinoic acid, which regulate the genes responsible for lipid metabolism and adipocyte differentiation. CRABP2 gene is located on chromosome 1q21-23 and this region has been linked with related disorders such as familial combined hyperlipidemia (FCHL) and type 2 diabetes mellitus.
CRABP proteins are of low molecular weight having an important function in retinoic acid-mediated regulation of human skin growth and differentiation.
Synonyms
RBP6, CRABP-II, CRABP2, RETINOIC ACID-BINDING PROTEIN CELLULAR TYPE II, Cellular retinoic acid-binding protein 2, Cellular retinoic acid-binding protein II.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MPNFSGNWKI IRSENFEELL KVLGVNVMLR KIAVAAASKP AVEIKQEGDT FYIKTSTTVR TTEINFKVGE EFEEQTVDGR PCKSLVKWES ENKMVCEQKL LKGEGPKTSW TRELTNDGEL ILTMTADDVV CTRVYVRE.

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

Description:

Insulin Like Growth Factor-1, Mutant E3R Human Recombinant

Insulin-Like Growth Factor-1.

Product # :

CYT-1217

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Quantity :

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Description

IGF1 E3R Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids (Gly49-Ala118) and having a molecular mass of 8.6kDa. IGF1 E3R Human is fused to a 6 a.a his tag at C-Terminus and is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The filtered (0.4µm) concentrated protein solution was lyophilized from 0.5mg/ml solution in 50 mM NaCl, 20 mM Tris and 5% (w/v) trehalose, pH 8.0.

Purity

Greater than 95% as determined by SDS-PAGE.

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Synonyms
Insulin-Like Growth Factor-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. IGF1 E3R is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MGPRTLCGAE LVDALQFVCG DRGFYFNKPT GYGSSSRRAP QTGIVDECCF RSCDLRRLEM YCAPLKPAKS AHHHHHH.
Background
Insulin-like Growth Factor 1 (IGF-1) is a critical peptide hormone that plays a central role in regulating growth and development. Genetic mutations in the IGF-1 gene can result in altered IGF-1 variants, leading to various physiological consequences. Understanding these IGF-1 mutants is of paramount importance as they offer insights into growth disorders, metabolic regulation, and potential therapeutic avenues. This research delves into the world of IGF-1 mutants, shedding light on their diverse functions and implications for human health.
The primary objective of this research is to elucidate the impact of IGF-1 mutations on growth regulation. In vitro and in vivo experiments will be conducted to investigate how these mutants interact with IGF-1 receptors, influence downstream signaling pathways, and modulate growth plate dynamics. Understanding these mechanisms is crucial for unraveling the complexities of growth disorders associated with IGF-1 mutations.
The second objective is to assess the clinical relevance of IGF-1 mutants in growth-related conditions. Clinical studies involving individuals with growth hormone deficiencies or growth disorders linked to IGF-1 mutations will be conducted to evaluate the effects of these mutants on stature and overall health. These investigations may provide valuable insights into potential therapeutic strategies for individuals affected by growth-related disorders.
The third objective is to explore the broader implications of IGF-1 mutants in metabolic regulation and age-related conditions. Research will investigate their roles in metabolic homeostasis, longevity, and susceptibility to age-related diseases. Understanding the multifaceted properties of IGF-1 mutants may open new avenues for therapeutic interventions in various health and aging-related conditions.
By delving into the diverse functions of IGF-1 mutants, this research aims to expand our understanding of their physiological roles and clinical applications. The findings may contribute to the development of targeted interventions for growth disorders, metabolic conditions, and age-related diseases.
What is the molecular weight/Mw of IGF1 E3R HUMAN Protein?
IGF1 E3R HUMAN Protein has a total Mw of 8.6kDa.

What is the source or expression system of IGF1 E3R HUMAN Protein?
Escherichia Coli.

What is the Purity of IGF1 E3R HUMAN Protein?
IGF1 E3R HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IGF1 E3R HUMAN Protein?
The biological functionality of IGF1 E3R HUMAN Protein will be determined in the future.

What is the amino acid sequence of IGF1 E3R HUMAN Protein?
MGPRTLCGAE LVDALQFVCG DRGFYFNKPT GYGSSSRRAP QTGIVDECCF RSCDLRRLEM YCAPLKPAKS AHHHHHH.

What applications can IGF1 E3R HUMAN Protein be used in?
IGF1 E3R HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IGF1 E3R HUMAN Protein?
The endotoxin level is minimal, IGF1 E3R HUMAN Protein was purified using conventional chromatography techniques.

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

Description:

Intercellular Adhesion Molecule-1 Human Recombinant, SF9

Intercellular Adhesion Molecule 1, Major Group Rhinovirus Receptor, ICAM-1, Intercellular Adhesion Molecule 1 (CD54), Human Rhinovirus Receptor, Cell Surface Glycoprotein P3.58, Human Rhinovirus Receptor, CD54 Antigen, P3.58, CD54, BB2, Intercellular adhesion molecule 1.

Product # :

PRO-2200

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Description

ICAM1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 692 amino acids (28-480a.a.) and having a molecular mass of 76.5kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). ICAM1 is expressed with a 239 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

ICAM1 protein solution (0.25mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The ED50 range ≤ 2 ug/ml is measured by the ability of the immobilized protein to support the adhesion of HL-60 human promyelocytic cells. When cells are added to Human ICAM-1/CD54 coated plates.

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Introduction
ICAM-1 also called CD54 is a single chain membrane glycoprotein expressed on the surface of a variety of non-haematopoietic and haematopoietic cell types and has roles in signal transduction, cell signaling and lymphocyte adhesion. ICAM1 binds to integrins such as CD11a / CD18, or CD11b / CD18. ICAM1 is also used by Rhinovirus as a receptor. ICAM-1 is an intercellular adhesion molecule constantly present in low concentrations in the membranes of leukocytes and endothelial cells. When stimulated by cytokine the concentrations significantly increase. ICAM-1 can be stimulated by interleukin-1 (IL-1) and tumor necrosis factor alpha (TNFA) and is expressed by the vascular endothelium, macrophages and lymphocytes. ICAM-1 is a ligand for LFA-1 which is a receptor found on leukocytes. Upon activation, leukocytes bind to endothelial cells via ICAM-1/LFA-1 and then transmigrate into tissues. ICAM-1 is implicated in subarachnoid hemorrhage (SAH). Levels of ICAM-1 are shown to be notably elevated in patients with SAH. Soluble ICAM-1 is detectable in the plasma and is elevated in patients with various inflammatory conditions.
Synonyms
Intercellular Adhesion Molecule 1, Major Group Rhinovirus Receptor, ICAM-1, Intercellular Adhesion Molecule 1 (CD54), Human Rhinovirus Receptor, Cell Surface Glycoprotein P3.58, Human Rhinovirus Receptor, CD54 Antigen, P3.58, CD54, BB2, Intercellular adhesion molecule 1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
QTSVSPSKVI LPRGGSVLVT CSTSCDQPKL LGIETPLPKK ELLLPGNNRK VYELSNVQED SQPMCYSNCP DGQSTAKTFL TVYWTPERVE LAPLPSWQPV GKNLTLRCQV EGGAPRANLT VVLLRGEKEL KREPAVGEPA EVTTTVLVRR DHHGANFSCR TELDLRPQGL ELFENTSAPY QLQTFVLPAT PPQLVSPRVL EVDTQGTVVC SLDGLFPVSE AQVHLALGDQ RLNPTVTYGN DSFSAKASVS VTAEDEGTQR LTCAVILGNQ SQETLQTVTI YSFPAPNVIL TKPEVSEGTE VTVKCEAHPR AKVTLNGVPA QPLGPRAQLL LKATPEDNGR SFSCSATLEV AGQLIHKNQT RELRVLYGPR LDERDCPGNW TWPENSQQTP MCQAWGNPLP ELKCLKDGTF PLPIGESVTV TRDLEGTYLC RARSTQGEVT REVTVNVLSP RYEVEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYRQKSL SLSPGKHHHH HH.
Background
Intercellular adhesion molecule-1 (ICAM-1) is a cell surface glycoprotein that plays a pivotal role in immune responses and inflammatory processes. This research aims to investigate the function and significance of ICAM-1 protein in various physiological and pathological conditions. Understanding the molecular mechanisms and regulatory roles of ICAM-1 can provide valuable insights into its potential as a therapeutic target for immune-related disorders.
Structure and Expression of ICAM-1 Protein:
ICAM-1 belongs to the immunoglobulin superfamily and is composed of five immunoglobulin-like domains. It is primarily expressed on the surfaces of endothelial cells, leukocytes, and other immune cells. ICAM-1 expression can be induced by pro-inflammatory cytokines, such as tumor necrosis factor-alpha (TNF-α) and interleukin-1 (IL-1), during immune responses and inflammatory conditions.
ICAM-1 and Leukocyte Adhesion:
One of the critical functions of ICAM-1 is its involvement in leukocyte adhesion and migration. ICAM-1 interacts with its primary receptor, lymphocyte function-associated antigen-1 (LFA-1), expressed on leukocytes. This interaction facilitates the firm adhesion of leukocytes to endothelial cells, leading to their transmigration into inflamed tissues. The ICAM-1/LFA-1 axis plays a crucial role in immune surveillance, inflammation, and host defense against pathogens.
Implications of ICAM-1 in Inflammatory Disorders:
ICAM-1 has been implicated in various inflammatory diseases, including rheumatoid arthritis, inflammatory bowel disease, and multiple sclerosis. Enhanced expression of ICAM-1 on endothelial cells promotes leukocyte recruitment and contributes to the perpetuation of chronic inflammation. Therefore, targeting ICAM-1-mediated leukocyte adhesion has emerged as a potential therapeutic strategy to alleviate inflammation and attenuate disease progression.
ICAM-1 in Viral Infections:
ICAM-1 also plays a role in viral infections, as several viruses exploit ICAM-1 to facilitate their entry into host cells. For instance, rhinoviruses, which cause the common cold, utilize ICAM-1 as a receptor for attachment and entry into respiratory epithelial cells. The interaction between ICAM-1 and viral proteins promotes viral internalization and subsequent infection. Understanding the mechanisms of ICAM-1-mediated viral entry can aid in the development of antiviral strategies.
Therapeutic Targeting of ICAM-1:
Given its crucial involvement in immune responses and disease pathogenesis, ICAM-1 has emerged as a potential therapeutic target. Strategies aimed at blocking ICAM-1/LFA-1 interactions have shown promise in preclinical and clinical studies. Monoclonal antibodies targeting ICAM-1 or LFA-1 have been developed to prevent leukocyte adhesion and reduce inflammation. Additionally, small molecule inhibitors and gene therapies targeting ICAM-1 expression are being explored as potential therapeutic interventions.
Challenges and Future Directions:
Although therapeutic targeting of ICAM-1 shows promise, several challenges need to be addressed. Specific targeting of ICAM-1 without affecting its physiological functions and potential off-target effects are important considerations. Additionally, the complex and dynamic nature of ICAM-1 expression and regulation require further investigation to optimize therapeutic strategies.
Conclusion:
The investigation of ICAM-1 protein provides insights into its pivotal role in immune responses, leukocyte adhesion, and inflammatory processes. Understanding the molecular mechanisms and functional implications of ICAM-1 opens avenues for the development of targeted therapies for inflammatory disorders and viral infections. Further research on ICAM-1 protein

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

Description:

soluble CD40 Ligand/TRAPMouse Recombinant, sf9

CD40 ligand, T-cell antigen Gp39, TNF-related activation protein, TRAP, Tumor necrosis factor ligand superfamily member 5, CD154, CD40lg, CD154, CD40-L, Cd40l, gp39, HIGM1, IGM, IMD3, Ly-62, Ly62, T-BAM, Tnfsf5.

Product # :

CYT-917

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Description

sCD40 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 155 amino acids (112-260 a.a.) and having a molecular mass of 17.2kDa (Migrates at 18-28kDa on SDS-PAGE under reducing conditions).sCD40 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

sCD40 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
CD40L or CD154 is a membrane glycoprotein and differentiation antigen expressed on the surface of T-cells. The CD40 ligand stimulates B-cell proliferation and secretion of all immunoglobulin isotypes in the presence of cytokines . CD40 ligand has been shown to induce cytokine production and tumoricidal activity in peripheral blood monocytes. It also costimulates proliferation of activated T-cells and this is accompanied by the production of IFN-gamma , TNF-alpha , and IL2.
Synonyms
CD40 ligand, T-cell antigen Gp39, TNF-related activation protein, TRAP, Tumor necrosis factor ligand superfamily member 5, CD154, CD40lg, CD154, CD40-L, Cd40l, gp39, HIGM1, IGM, IMD3, Ly-62, Ly62, T-BAM, Tnfsf5.
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
MQRGDEDPQI AAHVVSEANS NAASVLQWAK KGYYTMKSNL VMLENGKQLT VKREGLYYVY TQVTFCSNRE PSSQRPFIVG LWLKPSSGSE RILLKAANTH SSSQLCEQQS VHLGGVFELQ AGASVFVNVT EASQVIHRVG FSSFGLLKLH 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.

Description:

Triggering receptor expressed on myeloid cells 2, Mouse Anti Human

Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.

Product # :

ANT-429

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Formulation

1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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Introduction
TREM2 is a membrane protein that forms a receptor signaling complex with TYROBP. TREM2 may be involved in chronic inflammation by triggering the production of constitutive inflammatory cytokines. Defects in the TREM2 gene are a source of polycystic lipomembranous osteodysplasia with sclerosing leukoencephalopathy (PLOSL).
Synonyms
Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.
Immunogen
Anti-human TREM2 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human TREM2 amino acids 19-161 purified from E. coli.
Ig Subclass
Mouse IgG3 heavy chain and κ light chain.
Clone
P2B5AT.
Applications
TREM2 antibody has been tested by ELISA and Western blot 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 is 1:500 ~ 1,000.Recommended starting dilution is 1:500.
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
TREM2 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.

Description:

Pegylated Rat Leptin Recombinant

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-592

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Mono-Pegylated Leptin Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and an additional Ala at N-terminus having a molecular mass of 35.6 kDa (with 20 kDa PEG) as determined by mass spectometry. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 100 kDa protein. Its half-life in circulation after SC injection was over 20 hours. Rat Leptin was purified by proprietary chromatographic techniques according to Salomon et al (2006) Protein Expression and Purification 47, 128–136 and then pegylated.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

Purity

Greater than 99.0% as determined by:
(a) Analysis by Gel-Filtration.
(b) Analysis by SDS-PAGE.

Biological Activity

Pegylated Rat Leptin is capable of stimulatng proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is only slightly lower than the non-pegylated antagonist but in vivo it has profound weight reducing effect (as compared to the non-pegylated leptin), resulting mainly from reduced food intake.

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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized pegylated Rat Leptin Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution of pegylated Rat Leptin at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization Rat leptin can be stored at 4C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized pegylated Rat Leptin in sterile water or in sterile 0.4% NaHCO3 adjusted to pH-8.5, not less than 100µg/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.

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